Cited by 1,150Metal-Catalyzed Oxygenation MechanismsEnzyme Structure and FunctionMetalloenzymes and iron-sulfur proteins

The DOI matches its Crossref record; 72 of the 72 references it cites were found in a registry or an index.

Metal ions in biological catalysis: from enzyme databases to general principles

Andreini, Claudia, Bertini, Ivano, Cavallaro, Gabriele, Holliday, Gemma L., Thornton, Janet M.·2008·JBIC Journal of Biological Inorganic Chemistry

DOI 10.1007/s00775-008-0404-5

Open this paper in CoChat — free account

Abstract

We analysed the roles and distribution of metal ions in enzymatic catalysis using available public databases and our new resource Metal-MACiE (http://www.ebi.ac.uk/thornton-srv/databases/Metal_MACiE/home.html). In Metal-MACiE, a database of metal-based reaction mechanisms, 116 entries covering 21% of the metal-dependent enzymes and 70% of the types of enzyme-catalysed chemical transformations are annotated according to metal function. We used Metal-MACiE to assess the functions performed by metals in biological catalysis and the relative frequencies of different metals in different roles, which can be related to their individual chemical properties and availability in the environment. The overall picture emerging from the overview of Metal-MACiE is that redox-inert metal ions are used in enzymes to stabilize negative charges and to activate substrates by virtue of their Lewis acid properties, whereas redox-active metal ions can be used both as Lewis acids and as redox centres. Magnesium and zinc are by far the most common ions of the first type, while calcium is relatively less used. Magnesium, however, is most often bound to phosphate groups of substrates and interacts with the enzyme only transiently, whereas the other metals are stably bound to the enzyme. The most common metal of the second type is iron, which is prevalent in the catalysis of redox reactions, followed by manganese, cobalt, molybdenum, copper and nickel. The control of the reactivity of redox-active metal ions may involve their association with organic cofactors to form stable units. This occurs sometimes for iron and nickel, and quite often for cobalt and molybdenum.

Integrity signals

Registry

Crossref · 10.1007/s00775-008-0404-5

Cites

72 of 72 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides
Shannon, R. D. (1976) · Acta Crystallographica Section A · doi:10.1107/s0567739476001551 · Cited by 66,145
The Protein Data Bank
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
KEGG: Kyoto Encyclopedia of Genes and Genomes
Kanehisa, M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.27 · Cited by 37,077
KEGG: Kyoto Encyclopedia of Genes and Genomes
Ogata, H., Goto, S., Sato, K., Fujibuchi, W., Bono, H., & Kanehisa, M. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.29 · Cited by 31,232
Absolute hardness: companion parameter to absolute electronegativity
Parr, R. G., & Pearson, R. G. (1983) · Journal of the American Chemical Society · doi:10.1021/ja00364a005 · Cited by 7,998
Structural and Functional Aspects of Metal Sites in Biology
Holm, R. H., Kennepohl, P., & Solomon, E. I. (1996) · Chemical Reviews · doi:10.1021/cr9500390 · Cited by 2,573
Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates
Costas, M., Mehn, M. P., Jensen, M. P., & QUE, L. J. (2004) · Chemical Reviews · doi:10.1021/cr020628n · Cited by 2,478
MEROPS: the peptidase database
Rawlings, N. D., & Barrett, A. J. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.325 · Cited by 2,284
The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1996) · Science · doi:10.1126/science.272.5265.1136 · Cited by 2,102
The biological chemistry of the elements: the inorganic chemistry of life
(1992) · Choice Reviews Online · doi:10.5860/choice.30-0286 · Cited by 1,326

Flagged first, then by citations

Show all 72 references

Research works printed but not linked: 1

Luthi D, Gunzel D, McGuigan JA (1999) Exp Physiol 84:231–252

Sorted by citations

Items 301–400 of 1,000

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS
Lothian, A., & Roberts, B. R. (2016) · Journal of Visualized Experiments · doi:10.3791/53737 · Cited by 37
Purification and characterization of alkaline chitinase from Paenibacillus pasadenensis CS0611
Guo, X. C., Xu, P., Zong, M., & Lou, W. (2017) · CHINESE JOURNAL OF CATALYSIS (CHINESE VERSION) · doi:10.1016/s1872-2067(17)62787-6 · Cited by 37
Zinc-dependent substrate-level phosphorylation powers Salmonella growth under nitrosative stress of the innate host response
Fitzsimmons, L. F., Liu, L., Porwollik, S., Chakraborty, S., Desai, P., Tapscott, T., Henard, C. A., McClelland, M., & Vázquez‐Torres, A. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007388 · Cited by 37
Nickel (II) and cobalt (II) complexes with bidentate nitrogen-sulfur donor pyrazole derivative ligands: Syntheses, characterization, X-ray structure, electrochemical studies, and antibacterial activity
Soltani, B., Ghorbanpour, M., Ziegler, C. J., Ebadi-Nahari, M., & Mohammad‐Rezaei, R. (2020) · Polyhedron · doi:10.1016/j.poly.2020.114423 · Cited by 37
Staphylococcus aureus Pore-Forming Toxins
Robles, T. R., & Torres, V. J. (2016) · Current topics in microbiology and immunology · doi:10.1007/82_2016_16 · Cited by 39
Differential Effects of Iron, Zinc, and Copper on Dictyostelium discoideum Cell Growth and Resistance to Legionella pneumophila
Buracco, S., Peracino, B., Andreini, C., Bracco, E., & Bozzaro, S. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00536 · Cited by 36
Self-citation
Metal Homeostasis in Land Plants: A Perpetual Balancing Act Beyond the Fulfilment of Metalloproteome Cofactor Demands
Krämer, U. (2024) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-070623-105324 · Cited by 41
Speculative Volcanology
Clark, N., Gormally, A., & Tuffen, H. (2018) · Environmental Humanities · doi:10.1215/22011919-4385571 · Cited by 36
Alteration of the characteristics of extracellular polymeric substances (EPS) extracted from the fungus Phanerochaete chrysosporium when exposed to sub-toxic concentrations of nickel (II)
Cao, F., Bourven, I., Guibaud, G., Rene, E. R., Lens, P. N. L., Péchaud, Y., & van Hullebusch, E. D. (2018) · International Biodeterioration & Biodegradation · doi:10.1016/j.ibiod.2018.02.009 · Cited by 36
Antibacterial efficiency of alkali-free bio-glasses incorporating ZnO and/or SrO as therapeutic agents
Popa, A. C., Fernandes, H. R., Necşulescu, M., Luculescu, C. R., Cioangher, M., Dumitru, V., Stuart, B. W., Grant, D. M., Ferreira, J. M. F., & Stan, G. E. (2018) · Ceramics International · doi:10.1016/j.ceramint.2018.11.112 · Cited by 38
Metal-independent variants of phosphoglycerate mutase promote resistance to nutritional immunity and retention of glycolysis during infection
Radin, J. N., Kelliher, J. L., Solórzano, P. K. P., Grim, K. P., Ramezanifard, R., Slauch, J. M., & Kehl‐Fie, T. E. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007971 · Cited by 36
Regulatory effects of transition metals supplementation/deficiency on the gut microbiota
Li, C., Li, X., Shen, L., & Ji, H. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11096-2 · Cited by 35
Cornelian Cherry (Cornus masL.) Juices as a Source of Minerals in Human Diet
Krośniak, M., Gąstoł, M., Szałkowski, M., Zagrodzki, P., & Derwisz, M. (2010) · Journal of Toxicology and Environmental Health · doi:10.1080/15287394.2010.491408 · Cited by 36
Design Approaches That Utilize Ionic Interactions to Control Selectivity in Transition Metal Catalysis
Adams, H. K., Kadarauch, M., Hodson, N. J., Lit, A. R., & Phipps, R. J. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00849 · Cited by 35
Transport of Magnesium by a Bacterial Nramp-Related Gene
Shin, J., Wakeman, C. A., Goodson, J. R., Rodionov, D. A., Freedman, B. G., Senger, R. S., & Winkler, W. C. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004429 · Cited by 39
Metal regulation of metabolism
Bloom, A. J. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.09.017 · Cited by 35
Impact of transition metal ions on the structure and bioactivity of alkali-free bioactive glasses
Kapoor, S., Brazete, D. S., Pereira, I. F., Bhatia, G., Kaur, M., Santos, L. F., Banerjee, D., Goel, A., & Ferreira, J. M. F. (2019) · Journal of Non-Crystalline Solids · doi:10.1016/j.jnoncrysol.2018.12.003 · Cited by 35
Omics Integration for Mitochondria Systems Biology
Hu, X. Y., Go, Y., & Jones, D. P. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.8006 · Cited by 35
Crystal Structures Reveal that the Reaction Mechanism of Imidazoleglycerol-Phosphate Dehydratase Is Controlled by Switching Mn(II) Coordination
Bisson, C., Britton, K. L., Sedelnikova, S. E., Rodgers, H. F., Eadsforth, T. C., Viner, R. C., Hawkes, T. R., Baker, P. J., & Rice, D. W. (2015) · Structure · doi:10.1016/j.str.2015.05.012 · Cited by 35
Cellular Iron Distribution in Bacillus anthracis
Tu, W. Y., Pohl, S., Gray, J., Robinson, N. J., Harwood, C. R., & Waldron, K. J. (2012) · Journal of Bacteriology · doi:10.1128/jb.06195-11 · Cited by 34
Characterizing the complexity of enzymes on the basis of their mechanisms and structures with a bio-computational analysis
Holliday, G., Fischer, J. D., Mitchell, J. B. O., & Thornton, J. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08190.x · Cited by 39
Self-citation
Competition for Manganese at the Host–Pathogen Interface
Kelliher, J. L., & Kehl-Fie, T. E. (2016) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2016.05.002 · Cited by 34
The Fe and Zn cofactor dilemma
Chen, J., Calderone, L. A., Pan, L., Quist, T., & Pandelia, M. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140931 · Cited by 33
Transition Metal Homeostasis in Streptococcus pyogenes and Streptococcus pneumoniae
Turner, A. G., Ong, C. Y., Walker, M. J., Djoko, K. Y., & McEwan, A. G. (2017) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2017.01.002 · Cited by 35
PmtA functions as a ferrous iron and cobalt efflux pump in Streptococcus suis
Zheng, C., Jia, M., Gao, M., Lu, T., Li, L., & Zhou, P. (2019) · Emerging Microbes & Infections · doi:10.1080/22221751.2019.1660233 · Cited by 34
Biochemical and structural insights into 6-phosphogluconate dehydrogenase from Leishmania donovani
Jakkula, P., Narsimulu, B., & Qureshi, I. A. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11434-4 · Cited by 34
The structural basis of bacterial manganese import
Neville, S. L., Sjöhamn, J., Watts, J. A., MacDermott-Opeskin, H., Fairweather, S. J., Ganio, K., Hulyer, A. C., McGrath, A. P., Hayes, A. J., Malcolm, T. R., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg3980 · Cited by 33
Accurate Metal–Imidazole Interactions
Li, Z., Song, L. F., Sharma, G., Fındık, B. K., & Merz, K. M. (2022) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c01081 · Cited by 34
Outlining Potential Biomarkers of Exposure and Effect to Critical Minerals: Nutritionally Essential Trace Elements and the Rare Earth Elements
Jenkins, J. A., Musgrove, M., & White, S. J. O. (2023) · Toxics · doi:10.3390/toxics11020188 · Cited by 34
Improving microbial production of value-added products through the intervention of magnetic fields
Chen, S., Jin, Y., Yang, N., Wei, L., Xu, D., & Xu, X. (2023) · Bioresource Technology · doi:10.1016/j.biortech.2023.130087 · Cited by 33
Ecogenomic responses of benthic communities under multiple stressors along the marine and adjacent riverine areas of northern Bohai Sea, China
Xie, Y., Hong, S., Kim, S., Zhang, X., Yang, J., Giesy, J. P., Wang, T., Lü, Y., Yu, H., & Khim, J. S. (2016) · Chemosphere · doi:10.1016/j.chemosphere.2016.12.121 · Cited by 33
Dietary manganese requirement and its effects on antioxidant enzyme activities, intestinal morphology and microbiota in oriental river prawn Macrobrachium nipponense (De Haan)
Ding, Z., Chen, X., Kong, Y., Shao, X., Zhang, Y., & Ye, J. (2019) · Aquaculture · doi:10.1016/j.aquaculture.2019.734622 · Cited by 33
Metallohelices emulate the properties of short cationic α-helical peptides
Song, H. L., Postings, M. L., Scott, P., & Rogers, N. J. (2021) · Chemical Science · doi:10.1039/d0sc06412b · Cited by 34
How calcium inhibits the magnesium‐dependent kinase gsk3β: A molecular simulation study
Lu, S., Huang, Z., Huang, W., Liu, X., Chen, Y., Shi, T., & Zhang, J. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24221 · Cited by 33
Why is manganese so valuable to bacterial pathogens?
Čapek, J., & Večerek, B. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.943390 · Cited by 32
Relationship between Representative Trace Components and Health Functions of Chinese Baijiu: A Review
Du, P., Jiao, G., Zhang, Z., Wang, J., Li, P., Dong, J., & Wang, R. (2023) · Fermentation · doi:10.3390/fermentation9070658 · Cited by 33
A synergistic association between iron reduction and enhanced hydrogen production in Clostridium pasteurianum
Mishra, P., & Pradhan, N. (2024) · Biochemical Engineering Journal · doi:10.1016/j.bej.2024.109216 · Cited by 31
Synthesis, spectroscopic characterization, biological screening, and theoretical studies of organotin(IV) complexes of semicarbazone and thiosemicarbazones derived from (2-hydroxyphenyl)(pyrrolidin-1-yl)methanone
Singh, H. L., Singh, J., & Bhanuka, S. (2015) · Research on Chemical Intermediates · doi:10.1007/s11164-015-2069-3 · Cited by 32
Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds
Pinter, T. B. J., Koebke, K. J., & Pecoraro, V. L. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201907502 · Cited by 33
PRE‐driven protein NMR structures: an alternative approach in highly paramagnetic systems
Trindade, I. B., Invernici, M., Cantini, F., Louro, R. O., & Piccioli, M. (2020) · FEBS Journal · doi:10.1111/febs.15615 · Cited by 32
Is Ferroptosis a Future Direction in Exploring Cryptococcal Meningitis?
Xu, X., Lin, D., Tu, S., Gao, S., Shao, A., & Sheng, J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.598601 · Cited by 33
Thermostable alkaline phytase from Bacillus sp. MD2: Effect of divalent metals on activity and stability
Tran, T. T. T., Hashim, S. O., Gaber, Y., Mamo, G., Mattìasson, B., & Hatti‐Kaul, R. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.04.005 · Cited by 32
Zinc transfer from the embryo-specific metallothionein EC from wheat: a case study
Leszczyszyn, O. I., & Blindauer, C. A. (2010) · Physical Chemistry Chemical Physics · doi:10.1039/c0cp00680g · Cited by 32
Oxidation of Aldehydes into Carboxylic Acids by a Mononuclear Manganese(III) Iodosylbenzene Complex through Electrophilic C–H Bond Activation
Jeong, D., Kim, H., & Cho, J. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c09274 · Cited by 31
DNA photo-cleaving agents in the far-red to near-infrared range – a review
Li, Z., & Grant, K. B. (2016) · RSC Advances · doi:10.1039/c5ra28102d · Cited by 31
Use of Selenium-enriched olive leaves in the feed of growing rabbits: Effect on oxidative status, mineral profile and Selenium speciation of Longissimus dorsi meat
Mattioli, S., Bosco, A. D., Duarte, J. M. M., D’Amato, R., Castellini, C., Beone, G. M., Fontanella, M. C., Beghelli, D., Regni, L., Businelli, D., et al. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.10.004 · Cited by 31
Potential factors involved in the early pathogenesis of Streptococcus uberis mastitis: a review
Fessia, A. S., & Odierno, L. M. (2021) · Folia Microbiologica · doi:10.1007/s12223-021-00879-9 · Cited by 30
Nitrogen, Iron, and Zinc Acquisition: Key Nutrients to Aspergillus fumigatus Virulence
Perez‐Cuesta, U., Guruceaga, X., Cendon‐Sanchez, S., Pelegri‐Martinez, E., Hernando, F. L., Ramirez‐Garcia, A., Abad, A., & Rementerı́a, A. (2021) · Journal of Fungi · doi:10.3390/jof7070518 · Cited by 31
Host–Pathogen Interactions of Marine Gram-Positive Bacteria
Gnanagobal, H., & Santander, J. (2022) · Biology · doi:10.3390/biology11091316 · Cited by 36
Measuring copper and zinc superoxide dismutase from spinal cord tissue using electrospray mass spectrometry
Rhoads, T. W., Lopez, N. I., Zollinger, D. R., Morré, J. T., Arbogast, B. L., Maier, C. S., Denoyer, L. K., & Beckman, J. S. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.03.029 · Cited by 31
Enhancement of Escherichia coli bacterial biomass and hydrogen production by some heavy metal ions and their mixtures during glycerol vs glucose fermentation at a relatively wide range of pH
Trchounian, K. A., Poladyan, A. A., & Trchоunian, A. (2017) · International Journal of Hydrogen Energy · doi:10.1016/j.ijhydene.2017.02.003 · Cited by 31
Impact of Heavy Metals on Human Health
Parui, R., Nongthombam, G. S., Hossain, M., Adil, L. R., Gogoi, R., Bhowmik, S., Barman, D., & Iyer, P. K. (2023) · Wiley eBooks · doi:10.1002/9781119853589.ch4 · Cited by 31
Chronic Ethanol Exposure: Pathogenesis of Pulmonary Disease and Dysfunction
Traphagen, N. A., Tian, Z., & Allen‐Gipson, D. (2015) · Biomolecules · doi:10.3390/biom5042840 · Cited by 30
Zn2+ Uptake in Streptococcus pyogenes: Characterization of adcA and lmb Null Mutants
Tedde, V., Rosini, R., & Galeotti, C. L. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152835 · Cited by 30
Synthesis, characterization and antitumoral activity of new cobalt(II)complexes: Effect of the ligand isomerism on the biological activity of the complexes
Morcelli, S. R., Bull, É. S., Terra, W. D. S., Moreira, R. O., Borges, F. V., Kanashiro, M. M., Bortoluzzi, A. J., Maciel, L. L. F., Almeida, J. C. D. A., Horn, A., et al. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.05.003 · Cited by 30
Amide bond cleavage initiated by coordination with transition metal ions and tuned by an auxiliary ligand
Yang, Y., Lü, C., Wang, H., & Liu, X. (2016) · Dalton Transactions · doi:10.1039/c6dt01411a · Cited by 30
Magnetosensitivity of bacteria E. coli : Magnetic isotope and magnetic field effects
Letuta, U. G., & Berdinskiy, V. L. (2017) · Bioelectromagnetics · doi:10.1002/bem.22073 · Cited by 30
Evaluation of bioactive glass scaffolds incorporating SrO or ZnO for bone repair: In vitro bioactivity and antibacterial activity
Zhao, R., Shi, L., Gu, L., Qin, X., Song, Z., Fan, X., Zhao, P., Li, C., Zheng, H., Li, Z., et al. (2021) · Journal of Applied Biomaterials & Functional Materials · doi:10.1177/22808000211040910 · Cited by 30
MntP and YiiP Contribute to Manganese Efflux in Salmonella enterica Serovar Typhimurium under Conditions of Manganese Overload and Nitrosative Stress
Ouyang, A., Gasner, K. M., Neville, S. L., McDevitt, C. A., & Frawley, E. R. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.01316-21 · Cited by 29
Biofouling and biocorrosion by microbiota from a marine oil pipeline: A metagenomic and proteomic approach
Avelino-Jiménez, I. A., Hernández-Maya, L. G., Larios‐Serrato, V., Quej-Ake, L. M., Castelán-Sánchez, H., Herrera‐Díaz, J., Garibay-Feblés, V., Olvera, J. N. R., Olivares, G. Z., & Zapata‐Peñasco, I. (2023) · Journal of environmental chemical engineering · doi:10.1016/j.jece.2023.109413 · Cited by 30
Homology modeling andin vivofunctional characterization of the zinc permeation pathway in a heavy metal P-type ATPase
Lekeux, G., Crowet, J., Nouet, C., Joris, M., Jadoul, A., Bosman, B., Carnol, M., Motté, P., Lins, L., Galleni, M., et al. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/ery353 · Cited by 29
Rational Design of Enzymes
Pleiss, J. (2012) · Wiley eBooks · doi:10.1002/9783527639861.ch4 · Cited by 31
Biomimetic synergistic effect of redox site and Lewis acid for construction of efficient artificial enzyme
Si, H., Du, D., Jiao, C., Sun, Y., Li, L., & Tang, B. (2024) · Nature Communications · doi:10.1038/s41467-024-50687-1 · Cited by 31
Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source
Pishchany, G., Haley, K. P., & Skaar, E. P. (2013) · Journal of Visualized Experiments · doi:10.3791/50072 · Cited by 30
Agrobacterium tumefaciens Zur Regulates the High-Affinity Zinc Uptake System TroCBA and the Putative Metal Chaperone YciC, along with ZinT and ZnuABC, for Survival under Zinc-Limiting Conditions
Chaoprasid, P., Dokpikul, T., Johnrod, J., Sirirakphaisarn, S., Nookabkaew, S., Sukchawalit, R., & Mongkolsuk, S. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.00299-16 · Cited by 29
Efficient whole-cell catalysis for 5-aminovalerate production from L-lysine by using engineered Escherichia coli with ethanol pretreatment
Cheng, J., Luo, Q., Duan, H., Peng, H., Zhang, Y., Hu, J., & Lü, Y. (2020) · Scientific Reports · doi:10.1038/s41598-020-57752-x · Cited by 29
55/52Mn2+ Complexes with a Bispidine-Phosphonate Ligand: High Kinetic Inertness for Imaging Applications
Sy, M., Ndiaye, D., Silva, I. D., Lacerda, S., Charbonnière, L. J., Tóth, É., & Nonat, A. M. (2022) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.2c01681 · Cited by 29
Systematic analysis of biomolecular conformational ensembles with PENSA
Vögele, M., Thomson, N. J., Truong, S., McAvity, J., Zachariae, U., & Dror, R. O. (2025) · The Journal of Chemical Physics · doi:10.1063/5.0235544 · Cited by 27
Development and applications of the ABEEM fluctuating charge molecular force field in the ion-containing systems
Gong, L. (2012) · Science China Chemistry · doi:10.1007/s11426-012-4787-3 · Cited by 29
Influence of divalent magnesium ion on DNA: molecular dynamics simulation studies
Mukherjee, S., & Bhattacharyya, D. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.713780 · Cited by 30
The ColRS signal transduction system responds to the excess of external zinc, iron, manganese, and cadmium
Ainsaar, K., Mumm, K., Ilves, H., & Hõrak, R. (2014) · BMC Microbiology · doi:10.1186/1471-2180-14-162 · Cited by 29
Copper–zinc/chitosan complex hydrogels: Rheological, degradation and biological properties
Lončarević, A., Malbaša, Z., Kovačić, M., Ostojić, K., Angaïts, A., Skoko, Ž., Szpunar, J., Urlić, I., Ferrer, G. G., & Rogina, A. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.126373 · Cited by 28
Comparison of metal-binding strength between methionine and cysteine residues: Implications for the design of metal-binding motifs in proteins
Deepak, R. N. V. K., Chandrakar, B., & Sankararamakrishnan, R. (2017) · Biophysical Chemistry · doi:10.1016/j.bpc.2017.02.007 · Cited by 28
Disruption of Glycolysis by Nutritional Immunity Activates a Two-Component System That Coordinates a Metabolic and Antihost Response by Staphylococcus aureus
Solórzano, P. K. P., Yao, J., Rock, C. O., & Kehl‐Fie, T. E. (2019) · mBio · doi:10.1128/mbio.01321-19 · Cited by 34
Strategies for Zinc Uptake in Pseudomonas aeruginosa at the Host–Pathogen Interface
Wang, S., Cheng, J., Yanting, N., Li, P., Zhang, X., & Lin, J. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.741873 · Cited by 27
Automatic and accurate ligand structure determination guided by cryo-electron microscopy maps
Muenks, A., Zepeda, S., Zhou, G., Veesler, D., & DiMaio, F. (2023) · Nature Communications · doi:10.1038/s41467-023-36732-5 · Cited by 28
Efficient production of 5-aminovalerate from l-lysine by engineered Escherichia coli whole-cell biocatalysts
Wang, X., Cai, P., Chen, K., & Ouyang, P. (2016) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2016.10.008 · Cited by 28
Investigating the Campylobacter jejuni Transcriptional Response to Host Intestinal Extracts Reveals the Involvement of a Widely Conserved Iron Uptake System
Liu, M. M., Boinett, C. J., Chan, A., Parkhill, J., Murphy, M. E. P., & Gaynor, E. C. (2018) · mBio · doi:10.1128/mbio.01347-18 · Cited by 28
Targeting zinc homeostasis to combat Aspergillus fumigatus infections
Vicentefranqueira, R., Amich, J., Laskaris, P., Ibrahim-Granet, O., LatgÃ©, J. P., Toledo, H., Leal, F., & Calera, J. A. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00160 · Cited by 27
Rhizosphere priming and effects on mobilization and immobilization of multiple soil nutrients
Lu, J., Cai, J., Dijkstra, F. A., Yin, L., Wang, P., & Cheng, W. (2024) · Soil Biology and Biochemistry · doi:10.1016/j.soilbio.2024.109615 · Cited by 27
Production of a thermostable 1,3-1,4-β-glucanase mutant in Bacillus subtilis WB600 at a high fermentation capacity and its potential application in the brewing industry
Niu, C., Liu, C., Li, Y., Zheng, F., Wang, J., & Li, Q. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.08.139 · Cited by 27
Biochemistry of Copper Site Assembly in Heme-Copper Oxidases: A Theme with Variations
Llases, M., Morgada, M. N., & Vila, A. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153830 · Cited by 30
Synthetic biology approaches to copper remediation: bioleaching, accumulation and recycling
Giachino, A., Focarelli, F., Marles‐Wright, J., & Waldron, K. J. (2020) · FEMS Microbiology Ecology · doi:10.1093/femsec/fiaa249 · Cited by 28
Cysteine and iron accelerate the formation of ribose-5-phosphate, providing insights into the evolutionary origins of the metabolic network structure
Piedrafita, G., Varma, S. J., Castro, C., Messner, C. B., Szyrwiel, Ł., Griffin, J. L., & Ralser, M. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001468 · Cited by 27
Spectroscopic characterization, host-guest charge transfer, Hirshfeld surfaces, AIM-RDG and ELF study of adsorption and chemical sensing of heavy metals with new derivative of Calix [4]quinone: A DFT-D3 computation
Gassoumi, B., Mehri, A., Hammami, H., Castro, M. E., Karayel, A., Özkınalı, S., Meléndez, F. J., Nouar, L., Madi, F., Ghalla, H., et al. (2021) · Materials Chemistry and Physics · doi:10.1016/j.matchemphys.2021.125555 · Cited by 27
The Metal-binding Protein Atlas (MbPA): An Integrated Database for Curating Metalloproteins in All Aspects
Li, J., He, X., Gao, S., Liang, Y., Qi, Z., Xi, Q., Zuo, Y., & Xing, Y. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168117 · Cited by 27
Transition Metals and Organic Ligands Influence Biodegradation of 1,4-Dioxane
Pornwongthong, P., Mulchandani, A., Gedalanga, P. B., & Mahendra, S. (2014) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-014-0841-2 · Cited by 27
Database and tools for metabolic network analysis
Jing, L. S., Shah, F. F. M., Mohamad, M. S., Hamran, N. L., Salleh, A. H. M., Deris, S., & Alashwal, H. (2014) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-014-0172-8 · Cited by 28
The Rare-earth Metallome of Pecan and Other Carya
Wood, B. W., & Grauke, L. J. (2011) · Journal of the American Society for Horticultural Science · doi:10.21273/jashs.136.6.389 · Cited by 27
Intracellular zinc flux causes reactive oxygen species mediated mitochondrial dysfunction leading to cell death in Leishmania donovani
Kumari, A., Singh, K. P., Mandal, A., Paswan, R. K., Sinha, P., Das, P. K., Ali, V., Bimal, S., & Lal, C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178800 · Cited by 26
P-type transport ATPases inLeishmaniaandTrypanosoma
Meade, J. C. (2019) · Parasite · doi:10.1051/parasite/2019069 · Cited by 25
Involvement of the Pseudomonas aeruginosa MexAB–OprM efflux pump in the secretion of the metallophore pseudopaline
Gomez, N. O., Tetard, A., Ouerdane, L., Laffont, C., Brutesco, C., Ball, G., Łobiński, R., Denis, Y., Plésiat, P., Llanes, C., et al. (2020) · Molecular Microbiology · doi:10.1111/mmi.14600 · Cited by 24
Atomically Accurate Design of Metalloproteins with Predefined Coordination Geometries
Hoffnagle, A. M., & Tezcan, F. A. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c04047 · Cited by 27
Modulation of Quinone PCET Reaction by Ca 2+ Ion Captured by Calix[4]quinone in Water
Kim, Y., Kim, R. S., Kang, S. K., Choi, M. G., Kim, H. Y., Cho, D., Lee, J. Y., Chang, S.-K., & Chung, T. D. (2013) · Journal of the American Chemical Society · doi:10.1021/ja410406e · Cited by 26
Ferrihydrite Reduction Exclusively Stimulated Hydrogen Production by Clostridium with Community Metabolic Pathway Bifurcation
Zhang, Y., Xiao, L., Hao, Q., Li, X., & Liu, F. (2020) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.9b07702 · Cited by 27
Functional characterization of the ATPase-like activity displayed by a catalytic amyloid
Castillo-Caceres, C., Duran-Meza, E., Nova, E., Araya-Secchi, R. R., Monasterio, O., & Díaz‐Espinoza, R. (2020) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2020.129729 · Cited by 26
The Zinc Nutritional Immunity of Epinephelus coioides Contributes to the Importance of znuC During Pseudomonas plecoglossicida Infection
Huang, L., Zuo, Y., Qin, Y., Zhao, L., Lin, M., & Yan, Q. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.678699 · Cited by 26
Metals in Biology: From Metallomics to Trafficking
Buccella, D., Lim, M. H., & Morrow, J. R. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b02965 · Cited by 28
Mobilization of iron stored in bacterioferritin, a new target for perturbing iron homeostasis and developing antibacterial and antibiofilm molecules
Rivera, M. (2023) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2023.112306 · Cited by 27
The impact of manganese on vascular endothelium
Oliveira‐Paula, G. H., Martins, A. C., Ferrer, B., Tinkov, A. A., Skalny, A. V., & Aschner, M. (2024) · Toxicological Research · doi:10.1007/s43188-024-00260-1 · Cited by 26

Authors: Andreini, C., Bertini, I., Cavallaro, G., Holliday, G. L., & Thornton, J. M.
Affiliations: University of Florence (IT)
European Bioinformatics Institute (GB)
Corresponding author: Thornton, Janet M.
ORCID: Andreini, Claudia
Bertini, Ivano
Holliday, Gemma L.
Thornton, Janet M.
Venue: JBIC Journal of Biological Inorganic Chemistry
Publisher: Springer Science and Business Media LLC
Published: 2008-07-05
Volume: 13
Issue: 8
Pages: 1205-1218
ISSN: 0949-8257 (ISSN-L)
1432-1327
DOI: 10.1007/s00775-008-0404-5
OpenAlex: W2052498582
Cited by: 1,150
References: 72
Citations by year: 2026: 68 · 2025: 92 · 2024: 108 · 2023: 89 · 2022: 92 · 2021: 105 · 2020: 87 · 2019: 80 · 2018: 53 · 2017: 59 · 2016: 62 · 2015: 38 · 2014: 47 · 2013: 44 · 2012: 41
FWCI: 16.99
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: JBIC Journal of Biological Inorganic Chemistry (publishedVersion)
PubMed (publishedVersion)
BIROn (Birkbeck, University of London) (submittedVersion)
Florence Research (University of Florence) (submittedVersion)
Funders: Wellcome Trust (062347)
Topics: Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Keywords: metal ions, metalloenzymes, enzyme catalysis, redox-active metal ions, Lewis acid catalysis, magnesium, zinc, calcium, iron, manganese, cobalt, molybdenum, copper, nickel, cofactors
MeSH terms: Enzymes, Ions, Magnesium, Manganese, Metalloproteins, Metals, Models, Chemical, Oxidation-Reduction, Oxidoreductases, Transferases, Databases, Protein, Biocatalysis

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Metal ions in biological catalysis: from enzyme databases to general principles

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks