The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Nickel-based Enzyme Systems
Open accessAbstract
Of the eight known nickel enzymes, all but glyoxylase I catalyze the use and/or production of gases central to the global carbon, nitrogen, and oxygen cycles. Nickel appears to have been selected for its plasticity in coordination and redox chemistry and is able to cycle through three redox states (1+, 2+, 3+) and to catalyze reactions spanning approximately 1.5 V. This minireview focuses on the catalytic mechanisms of nickel enzymes, with an emphasis on the role(s) of the metal center. The metal centers vary from mononuclear to complex metal clusters and catalyze simple hydrolytic to multistep redox reactions.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Figures


Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“This is an important similarity to modern anaerobic autotrophs, whose enzymes of core carbon and energy pathways are replete with FeS, FeNiS and MoS (WS) centres, FeS and NiS usually being incorporated into proteins via cysteine residues [54–58], Mo and W usually being complexed by thiols of the molybdopterin cofactor MoCo [59].”
From Early bioenergetic evolution (2013) · cites this paper as [56]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In the enzymatic mechanism [56], electrons from a low-potential Fd are used by the enzyme to reduce one molecule of CO2 to CO at an FeNiS cluster called the C cluster; that CO migrates to a second FeNiS cluster in the enzyme (the A cluster), where it binds one of two Ni atoms at the Nip site to form a Ni-bound carbonyl group, where the two-electron donating property of Ni is important in the”
From Early bioenergetic evolution (2013) · cites this paper as [56]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“The catalysis in CODH/ACS is performed by transition metals (Fe and Ni) coordinated as sulfide clusters [50,56,73].”
From Early bioenergetic evolution (2013) · cites this paper as [56]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Kadish, K. M., Smith, K. M., & Guilard, R. (2003) · Elsevier eBooks · doi:10.1016/c2009-0-22714-0 · Cited by 2,594
Zelko, I. N., Mariani, T. J., & Folz, R. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00905-x · Cited by 2,212
Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
Vignais, P. M., & Billoud, B. (2007) · Chemical Reviews · doi:10.1021/cr050196r · Cited by 1,617
Acetogenesis and the Wood–Ljungdahl pathway of CO2 fixation
Ragsdale, S. W., & Pierce, E. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.08.012 · Cited by 1,409
Self-citationNickel essentiality, toxicity, and carcinogenicity
Denkhaus, E., & Salnikow, K. (2002) · Critical Reviews in Oncology/Hematology · doi:10.1016/s1040-8428(01)00214-1 · Cited by 1,134
Jack bean urease (EC 3.5.1.5). Metalloenzyme. Simple biological role for nickel
Dixon, N. E., Gazzola, C., Blakeley, R. L., & Zerner, B. (1975) · Journal of the American Chemical Society · doi:10.1021/ja00847a045 · Cited by 833
On the origin of biochemistry at an alkaline hydrothermal vent
Martin, W., & Russell, M. J. (2007) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2006.1881 · Cited by 771
Moore, G. R. (2002) · Journal of Organometallic Chemistry · doi:10.1016/s0022-328x(02)01715-1 · Cited by 701
Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation
Ermler, U., Grabarse, W., Shima, S., Goubeaud, M., & Thauer, R. K. (1997) · Science · doi:10.1126/science.278.5342.1457 · Cited by 615
Cited by
Sorted by citations
Items 101–200 of 400
Ferentinos, E., Maganas, D., Raptopoulou, C. P., Terzis, A., Psycharis, V., Robertson, N., & Kyritsis, P. (2010) · Dalton Transactions · doi:10.1039/c0dt00928h · Cited by 38
Native metals, electron bifurcation, and CO2 reduction in early biochemical evolution
Sousa, F. L., Preiner, M., & Martin, W. F. (2018) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.12.010 · Cited by 44
Haake, M., Reuillard, B., Chavarot‐Kerlidou, M., Costentin, C., & Artero, V. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202413910 · Cited by 38
Chatterjee, S. K., Roy, S., Barman, S. K., Maji, R. C., Olmstead, M. M., & Patra, A. K. (2012) · Inorganic Chemistry · doi:10.1021/ic300606g · Cited by 36
Influence of Ligand Flexibility on the Electronic Structure of Oxidized NiIII-Phenoxide Complexes
Kawai, M., Yamaguchi, T., Masaoka, S., Tani, F., Kohzuma, T., Chiang, L., Storr, T., Mieda, K., Ogura, T., Szilagyi, R. K., et al. (2014) · Inorganic Chemistry · doi:10.1021/ic501181k · Cited by 36
Aerobic CO Oxidation of a Metal-Bound Carbonyl in a NHC-Stabilized Cobalt Half-Sandwich Complex
Dürr, S., Zarzycki, B., Ertler, D., Ivanović‐Burmazović, I., & Radius, U. (2012) · Organometallics · doi:10.1021/om201037w · Cited by 36
Physiology, phylogeny, early evolution, and GAPDH
Martin, W. F., & Cerff, R. (2017) · PROTOPLASMA · doi:10.1007/s00709-017-1095-y · Cited by 36
Chen, Q., Chen, H., Johs, A., Lu, X., An, J., Pierce, E. M., Parks, J. M., Elias, D. A., Hettich, R. L., & Gu, B. (2018) · PROTEOMICS · doi:10.1002/pmic.201700479 · Cited by 36
Botana, L. M., Ruiz, J., Mota, A. J., Rodríguez‐Diéguez, A., Seco, J. M., Oyarzabal, I., & Colacio, E. (2014) · Dalton Transactions · doi:10.1039/c4dt01253d · Cited by 35
Naphthyridine derived colorimetric and fluorescent turn off sensors for Ni2+ in aqueous media
Ashraf, A., Islam, M. F., Khalid, M., Davis, A. P., Ahsan, M. T., Yaqub, M., Syed, A., Elgorban, A. M., Bahkali, A. H., & Shafiq, Z. (2021) · Scientific Reports · doi:10.1038/s41598-021-98400-2 · Cited by 35
Kumar, V., Singh, D., Kumar, P., Chaudhary, G., Singh, A. P., & Gupta, R. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.132901 · Cited by 35
Gennari, M., Orio, M., Pécaut, J., Bothe, E., Neese, F., Collomb, M., & Duboc, C. (2011) · Inorganic Chemistry · doi:10.1021/ic200063d · Cited by 35
Oyarzabal, I., Ruiz, J., Mota, A. J., Rodríguez‐Diéguez, A., Seco, J. M., & Colacio, E. (2015) · Dalton Transactions · doi:10.1039/c5dt00356c · Cited by 34
Maturation of the [Ni–4Fe–4S] active site of carbon monoxide dehydrogenases
Merrouch, M., Benvenuti, M., Lorenzi, M., Léger, C., Fourmond, V., & Dementin, S. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1541-0 · Cited by 34
An investigation of possible competing mechanisms for Ni-containing methyl–coenzyme M reductase
Chen, S., Blomberg, M. R. A., & Siegbahn, P. E. M. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp01483a · Cited by 34
Manesis, A. C., & Shafaat, H. S. (2015) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5b01103 · Cited by 34
Bano, B., Kanwal, Khan, K. M., Lodhi, M. A., Salar, U., Begum, F., Ali, M., Taha, M., & Perveen, S. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.06.007 · Cited by 34
Superoxide dismutase in Arabidopsis and Chlamydomonas: diversity, localization, regulation, and role
Shams, M., Pokora, W., Khadivi, A., & Aksmann, A. (2024) · Plant and Soil · doi:10.1007/s11104-024-06618-6 · Cited by 37
Lapointe, S., Khaskin, E., Fayzullin, R. R., & Khusnutdinova, J. R. (2019) · Organometallics · doi:10.1021/acs.organomet.9b00558 · Cited by 33
Hossain, M. E., Hasan, M. M., Halim, M. E., Ehsan, M. Q., & Halim, M. A. (2014) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2014.11.084 · Cited by 31
Horn, B., Limberg, C., Herwig, C., & Braun, B. (2014) · Inorganic Chemistry · doi:10.1021/ic500698v · Cited by 32
Sharma, V., Sahu, M., Manna, A. K., De, D., & Patra, G. K. (2022) · RSC Advances · doi:10.1039/d2ra05564c · Cited by 31
Wang, J., Wu, R., Liu, Z., Qi, L., Xu, H., Yang, H., Li, Y., Liu, L., Feng, G., & Zhang, L. (2024) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c15938 · Cited by 30
Yang, S., Kelly, R. L., Bian, X., Conway, T. M., Huang, K., Ho, T., Neibauer, J. A., Keil, R. G., Moffett, J. W., & John, S. G. (2021) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2021.07.004 · Cited by 30
GTP before ATP: The energy currency at the origin of genes
Mrnjavac, N., & Martin, W. F. (2024) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2024.149514 · Cited by 31
Mansor, M., Winkler, C. R., Hochella, M. F., & Xu, J. (2019) · Frontiers in Earth Science · doi:10.3389/feart.2019.00151 · Cited by 30
Quinoxaline-based chromogenic and fluorogenic chemosensors for the detection of metal cations
da Silva, L. C., Machado, V. G., & Menezes, F. G. (2021) · Chemical Papers · doi:10.1007/s11696-020-01484-9 · Cited by 29
Responses of Lactic Acid Bacteria to Heavy Metal Stress
Solioz, M., Mermod, M., Abicht, H. K., & Mancini, S. (2011) · Springer eBooks · doi:10.1007/978-0-387-92771-8_9 · Cited by 29
Musiani, F., Bertoša, B., Magistrato, A., Zambelli, B., Turano, P., Losasso, V., Micheletti, C., Ciurli, S., & Carloni, P. (2010) · Journal of Chemical Theory and Computation · doi:10.1021/ct900635z · Cited by 29
Application and Limitations of Nanocasting in Metal–Organic Frameworks
Malonzo, C. D., Wang, Z., Duan, J., Zhao, W., Webber, T. E., Li, Z., Kim, I. S., Kumar, A., Bhan, A., Platero‐Prats, A. E., et al. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b03181 · Cited by 28
On the Structure and Reaction Mechanism of Human Acireductone Dioxygenase
Miłaczewska, A., Kot, E., Amaya, J. A., Makris, T. M., Zając, M., Korecki, J., Chumakov, A. I., Trzewik, B., Kędracka–Krok, S., Minor, W., et al. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201704617 · Cited by 28
Zhang, M., Fan, Z., Hu, Z., & Luo, X. (2020) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2020.143458 · Cited by 28
Benini, S., Cianci, M., & Ciurli, S. (2011) · Dalton Transactions · doi:10.1039/c1dt11107h · Cited by 28
Manesis, A. C., Musselman, B. W., Keegan, B. C., Shearer, J., Lehnert, N., & Shafaat, H. S. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b03546 · Cited by 29
Kisgeropoulos, E. C., Manesis, A. C., & Shafaat, H. S. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c10135 · Cited by 26
Pyle, G. G., & Couture, P. (2011) · Fish physiology · doi:10.1016/s1546-5098(11)31005-9 · Cited by 26
Kim, H. M., Ahn, B., Lee, J.-H., & Roe, J. (2015) · Metallomics · doi:10.1039/c4mt00318g · Cited by 25
Nickel-responsive regulation of two novelHelicobacter pyloriNikR-targeted genes
Jones, M. D., Ademi, I., Yin, X., Gong, Y., & Zamble, D. B. (2014) · Metallomics · doi:10.1039/c4mt00210e · Cited by 25
Ni2+ effects on Nicotiana tabacum L. pollen germination and pollen tube growth
Breygina, M., Matveyeva, N. P., Polevova, S., Meychik, N., Nikolaeva, Y. I., Mamaeva, A. S., & Yermakov, I. P. (2012) · BioMetals · doi:10.1007/s10534-012-9584-0 · Cited by 24
Theoretical Studies of Nickel-Dependent Enzymes
Siegbahn, P. E. M., Chen, S., & Liao, R. (2019) · Inorganics · doi:10.3390/inorganics7080095 · Cited by 25
Mineral Nutrition of Plants Under Soil Water Deficit Condition: A Review
Bhattacharya, A. (2021) · Springer eBooks · doi:10.1007/978-981-33-6276-5_4 · Cited by 24
Nickel isotopic composition of the upper continental crust
Wu, G., Zhu, J., Wang, X., Johnson, T. M., He, Y., Huang, F., Wang, L., & Lai, S. (2022) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2022.06.019 · Cited by 24
Sasaki, M., Inoue, M., Katada, Y., & Taguchi, T. (2011) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2011.10.061 · Cited by 24
Structural and Functional Aspects of Metal Binding Sites in Natural and Designed Metalloproteins
Maglio, O., Nastri, F., & Lombardi, A. (2012) · Wiley eBooks · doi:10.1002/9781118165850.ch11 · Cited by 24
Complexes of Ni( ii ) and Cu( ii ) with small peptides: deciding whether to deprotonate
Dunbar, R. C., Martens, J. K., Berden, G., & Oomens, J. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp03974j · Cited by 23
Gond, M. K., Pandey, S. K., Singh, R. K., Bharty, M. K., Manna, P. P., Singh, V. K., Maiti, B., Prasad, L. B., & Butcher, R. J. (2022) · New Journal of Chemistry · doi:10.1039/d2nj00264g · Cited by 23
Nickel superoxide dismutase protects nitrogen fixation in Trichodesmium
Chen, C., Rodriguez, I. B., Chen, Y. L., Zehr, J. P., Chen, Y., Hsu, S. D., Yang, S., & Ho, T. (2022) · Limnology and Oceanography Letters · doi:10.1002/lol2.10263 · Cited by 23
The coenzyme/protein pair and the molecular evolution of life
Kirschning, A. (2020) · Natural Product Reports · doi:10.1039/d0np00037j · Cited by 23
Nwokolo, N. L., & Enebe, M. C. (2022) · Biomass Conversion and Biorefinery · doi:10.1007/s13399-022-02580-4 · Cited by 22
Banerjee, A., Guha, A., Maiti, P., Goswami, S., Chattopadhyay, T., Mondal, T. K., Bhattacharya, S., Zangrando, E., & Das, D. (2011) · Transition Metal Chemistry · doi:10.1007/s11243-011-9537-4 · Cited by 22
Zine, H., Rifai, L. A., Faize, M., Bentiss, F., Guesmi, S., Laachir, A., Smaili, A., Makroum, K., Sahibed-Dine, A., & Koussa, T. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b00151 · Cited by 22
From NAD+ to Nickel Pincer Complex: A Significant Cofactor Evolution Presented by Lactate Racemase
Yu, M., & Chen, S. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201700405 · Cited by 21
Glover, M. S., Dilger, J. M., Zhu, F., & Clemmer, D. E. (2013) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2013.06.014 · Cited by 21
Manganese, molybdenum, boron, silicon, and other trace elements
Nielsen, F. H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-323-66162-1.00029-9 · Cited by 20
Kaur, G., Singh, I., Tandon, N., Tandon, R., & Bhat, A. A. (2023) · ChemistrySelect · doi:10.1002/slct.202301661 · Cited by 21
Cation distribution and mixing thermodynamics in Fe/Ni thiospinels
Haider, S., Grau‐Crespo, R., Devey, A. J., & de Leeuw, N. H. (2012) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2012.04.007 · Cited by 20
Insights into the dioxygen activation and catalytic mechanism of the nickel-containing quercetinase
Li, H., Wang, X., Tian, G., & Liu, Y. (2018) · Catalysis Science & Technology · doi:10.1039/c8cy00187a · Cited by 20
Deciphering the chemoselectivity of nickel-dependent quercetin 2,4-dioxygenase
Wang, W.-J., Wei, W., & Liao, R. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp02683a · Cited by 20
Distribution and Cycling of Nickel and Nickel Isotopes in the Pacific Ocean
Bian, X., Yang, S., Raad, R. J., Odendahl, C. E., Lanning, N. T., Sieber, M., Huang, K., Fitzsimmons, J. N., Conway, T. M., & John, S. G. (2024) · Geophysical Research Letters · doi:10.1029/2024gl111115 · Cited by 19
Selective Turn-On Fluorescence Sensing of Cyanide Using the Pyridoxal Platform of a Ni(II) Complex
Mondal, A., & Chattopadhyay, S. K. (2022) · ACS Omega · doi:10.1021/acsomega.2c04063 · Cited by 19
Appended Lewis Acids Enable Dioxygen Reactivity and Catalytic Oxidations with Ni(II)
Beagan, D. M., Rivera, C., & Szymczak, N. K. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12399 · Cited by 19
Nickel's behaviour in marine sediments under aerobic to anaerobic diagenetic conditions
Bruggmann, S., McManus, J., Archer, C., Vance, D., & Severmann, S. (2024) · Chemical Geology · doi:10.1016/j.chemgeo.2024.122234 · Cited by 19
Methane oxidation in heavy metal contaminated Mollic Gleysol under oxic and hypoxic conditions
Walkiewicz, A., Bulak, P., Brzezińska, M., Wnuk, E., & Bieganowski, A. (2016) · Environmental Pollution · doi:10.1016/j.envpol.2016.02.048 · Cited by 19
Svane, S., & Karring, H. (2019) · Cogent Chemistry · doi:10.1080/23312009.2019.1644702 · Cited by 19
Stability Constants of Mixed Ligand Complexes of Nickel(II) with Adenine and Some Amino Acids
Türkel, N. (2015) · Bioinorganic Chemistry and Applications · doi:10.1155/2015/374782 · Cited by 18
Wang, B., & Shaik, S. S. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201612065 · Cited by 18
Small Molecule Activation at the acri PNP Pincer-Supported Nickel Sites
Park, S., Lee, K., Padmanaban, S., & Lee, Y. (2024) · Accounts of Chemical Research · doi:10.1021/acs.accounts.4c00401 · Cited by 18
Sfriso, A., Chiesa, S., Sfriso, A., Buosi, A., Gobbo, L., Gnolo, A. B., & Argese, E. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.06.057 · Cited by 18
Ghosh, T. K., Mahapatra, P., Jana, S., & Ghosh, A. (2019) · CrystEngComm · doi:10.1039/c9ce00574a · Cited by 18
Crisponi, G., & Nurchi, V. M. (2015) · Wiley eBooks · doi:10.1002/9781119951438.eibc0126.pub2 · Cited by 18
Nickel and zinc micronutrient availability in Phanerozoic oceans
Sweere, T., Dickson, A. J., & Vance, D. (2022) · Geobiology · doi:10.1111/gbi.12541 · Cited by 17
Karmakar, M., Das, R., & Chattopadhyay, S. (2024) · Inorganica Chimica Acta · doi:10.1016/j.ica.2024.122106 · Cited by 17
Wasylenki, L. E., Wells, R. M., Spivak-Birndorf, L. J., Baransky, E. J., & Frierdich, A. J. (2024) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2024.06.022 · Cited by 17
Carr, C. E., Musiani, F., Huang, H.-T., Chivers, P. T., Ciurli, S., & Maroney, M. J. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b00527 · Cited by 17
Martin, D., Alnajjar, P., Muselet, D., Soligot, C., Kanso, H., Pacaud, S., Roux, Y. L., Saaidi, P., & Feidt, C. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.166345 · Cited by 16
Potassium Is Critical for the Ni(II)-Responsive DNA-Binding Activity of Escherichia coli NikR
Wang, S. C., Li, Y., Robinson, C. V., & Zamble, D. B. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909136h · Cited by 16
Banerjee, K., Biswas, M. K., & Choudhuri, S. K. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-017-1498-4 · Cited by 16
Bio-inspired Ni dinuclear complexes as heterogeneous catalysts for hydrogen evolution
Cabrera-García, A., Blay, V., Blay-Roger, R., Ravelo, Á. G., González‐Platas, J., Arévalo, M. C., Sanchiz, J., & Martín-Zarza, P. (2021) · Chemical Engineering Journal · doi:10.1016/j.cej.2021.130342 · Cited by 16
Involvement of Ca2+ and ROS signals in nickel-impaired human sperm function
Chen, C., Li, B., Huang, R., Dong, S., Zhou, Y., Song, J., Zeng, X., & Zhang, X. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.113181 · Cited by 16
Nanomaterial-functionalized Cellulose: Design, Characterization and Analytical Applications
Kirk, K. A., Othman, A. A., & Andreescu, S. (2018) · Analytical Sciences · doi:10.2116/analsci.34.19 · Cited by 16
Meuser, M. V. M., Quattrociocchi, D. G. S., da Costa, L. M., Ferreira, G. B., & Carneiro, J. W. D. M. (2015) · Polyhedron · doi:10.1016/j.poly.2015.09.059 · Cited by 15
Shimazaki, Y., & Yamauchi, O. (2012) · Chemistry & Biodiversity · doi:10.1002/cbdv.201100446 · Cited by 15
Synchrotron-based Nickel Mössbauer Spectroscopy
Gee, L. B., Lin, C., Jenney, F. E., Adams, M. W. W., Yoda, Y., Masuda, R., Saito, M., Kobayashi, Y., Tamasaku, K., Lerche, M., et al. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5b03004 · Cited by 15
Tan, X., Chen, H., Gu, C., Zang, J., Zhang, T., Wang, H., & Zhao, G. (2020) · Communications Chemistry · doi:10.1038/s42004-020-00394-x · Cited by 15
A high-spin nickel( ii ) borohydride complex in dehalogenation
Tak, H., Lee, H., Kang, J., & Cho, J. (2015) · Inorganic Chemistry Frontiers · doi:10.1039/c5qi00206k · Cited by 15
Vujović, M., Huynh, M. T., Steiner, S., García‐Fernández, P., Elstner, M., Cui, Q., & Gruden, M. (2018) · Journal of Computational Chemistry · doi:10.1002/jcc.25614 · Cited by 15
Process Analysis of Anaerobic Fermentation Exposure to Metal Mixtures
Tian, Y., Zhang, H., Zheng, L., Li, S., Hao, H., Yin, M., Cao, Y., & Huang, H. (2019) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph16142458 · Cited by 16
Wang, H., Chen, Y., Ji, J., Li, X., Hedding, D. W., & Chen, J. (2023) · Geoderma · doi:10.1016/j.geoderma.2023.116494 · Cited by 15
Herritsch, J., Luy, J., Rohlf, S., Gruber, M., Klein, B. P., Kalläne, M., Schweyen, P., Bröring, M., Roßnagel, K., Tonner, R., et al. (2020) · ECS Journal of Solid State Science and Technology · doi:10.1149/2162-8777/ab9e18 · Cited by 14
Zhang, T., Zhang, X., & Chung, L. W. (2018) · Asian Journal of Organic Chemistry · doi:10.1002/ajoc.201700645 · Cited by 14
Lihi, N., Csire, G., Szakács, B., May, N. V., Várnagy, K., Sóvágó, I., & Fábián, I. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b02952 · Cited by 15
Fukushima, Y., & Aikawa, S. (2019) · Tetrahedron Letters · doi:10.1016/j.tetlet.2019.01.055 · Cited by 14
Metal stable isotopes in the marine realm
Little, S., de Souza, G. F., & Xie, R. C. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-99762-1.00019-x · Cited by 16
Inoue, M., Sasaki, M., Katada, Y., & Taguchi, T. (2013) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.32982 · Cited by 13
Introduction to the Biological Chemistry of Nickel
Zamble, D. B. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781788010580-00001 · Cited by 15
Nickel Exposure Has Complex Transgenerational Effects in a Butterfly
Kobiela, M. E., & Snell‐Rood, E. C. (2018) · Integrative and Comparative Biology · doi:10.1093/icb/icy096 · Cited by 13
The Bioinorganic Chemistry of the First Row d-Block Metal Ions—An Introduction
Marques, H. M. (2025) · Inorganics · doi:10.3390/inorganics13050137 · Cited by 14
Sondermann, C., & Ringenberg, M. R. (2017) · Dalton Transactions · doi:10.1039/c7dt00960g · Cited by 12
De, A., Dey, D., Pal, C. K., Paul, S., & Biswas, B. (2019) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2019.05.121 · Cited by 12
Bhandari, A., Mishra, S., Maji, R. C., Kumar, A., Olmstead, M. M., & Patra, A. K. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202001363 · Cited by 12
Metadata
- Authors
- Ragsdale, S. W.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Ragsdale, Stephen W.
- ORCID
- Ragsdale, Stephen W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-07
- Volume
- 284
- Issue
- 28
- Pages
- 18571-18575
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2707248
- OpenAlex
- W1996983125
- Cited by
- 400
- References
- 40
- Citations by year
- 2026: 24 · 2025: 32 · 2024: 39 · 2023: 26 · 2022: 30 · 2021: 24 · 2020: 24 · 2019: 26 · 2018: 26 · 2017: 20 · 2016: 11 · 2015: 15 · 2014: 26 · 2013: 22 · 2012: 23
- FWCI
- 0.95
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM039451)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- nickel enzymes, nickel coordination chemistry, redox state, catalytic mechanism, metal centers, metal clusters, carbon cycle, nitrogen cycling, oxygen cycle, hydrolysis
- MeSH terms
- Acetate-CoA Ligase, Biochemistry, Carbon, Catalysis, Enzymes, Hydrogenase, Hydrolysis, Metals, Models, Molecular, Molecular Conformation, Nickel, Nitrogen, Oxidation-Reduction, Oxygen, Urease
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