Staphylococcus aureus heme and siderophore-iron acquisition pathways

Siderophore-Based Iron Acquisition and Pathogen Control

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Chemistry and biology of siderophores

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Iron Metabolism in Pathogenic Bacteria

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Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

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Iron in infection and immunity

Cassat, J. E., & Skaar, E. P. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.04.010 · Cited by 1,214 · see citing works

Enterobactin: an archetype for microbial iron transport.

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Iron homeostasis in host defence and inflammation

Ganz, T., & Nemeth, E. (2015) · Nature Reviews Immunology · doi:10.1038/nri3863 · Cited by 843 · see citing works

Genetics and Assembly Line Enzymology of Siderophore Biosynthesis in Bacteria

Crosa, J. H., & Walsh, C. T. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.2.223-249.2002 · Cited by 797 · see citing works

Passage of Heme-Iron Across the Envelope of <i>Staphylococcus aureus</i>

Mazmanian, S. K., Skaar, E. P., Gaspar, A. H., Humayun, M., Gornicki, P., Jelenska, J., Joachmiak, A., Missiakas, D. M., & Schneewind, O. (2003) · Science · doi:10.1126/science.1081147 · Cited by 593 · see citing works

A structural classification of substrate‐binding proteins

Berntsson, R. P. ‐., Smits, S. H. J., Schmitt, L., Slotboom, D.-J., & Poolman, B. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.043 · Cited by 552 · see citing works

A U.S. Population-Based Survey of Staphylococcus aureus Colonization

Graham, P. L., Lin, S. X., & Larson, E. (2006) · Annals of Internal Medicine · doi:10.7326/0003-4819-144-5-200603070-00006 · Cited by 458 · see citing works

Iron-Source Preference of <i>Staphylococcus aureus</i> Infections

Skaar, E. P., Humayun, M., Bae, T., DeBord, K. L., & Schneewind, O. (2004) · Science · doi:10.1126/science.1099930 · Cited by 440 · see citing works

An iron-regulated sortase anchors a class of surface protein during <i>Staphylococcus aureus</i> pathogenesis

Mazmanian, S. K., Ton-That, H., Su, K., & Schneewind, O. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032523999 · Cited by 372 · see citing works

Nutritional Immunity: Host's Attempt to Withhold Iron From Microbial Invaders

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A Widely Distributed Bacterial Pathway for Siderophore Biosynthesis Independent of Nonribosomal Peptide Synthetases

Challis, G. L. (2005) · ChemBioChem · doi:10.1002/cbic.200400283 · Cited by 323 · see citing works

Vaccine assembly from surface proteins of <i>Staphylococcus aureus</i>

Stranger-Jones, Y. K., Bae, T., & Schneewind, O. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606863103 · Cited by 309 · see citing works

<i>Staphylococcus aureus</i> IsdB Is a Hemoglobin Receptor Required for Heme Iron Utilization

Torres, V. J., Pishchany, G., Humayun, M., Schneewind, O., & Skaar, E. P. (2006) · Journal of Bacteriology · doi:10.1128/jb.01335-06 · Cited by 302 · see citing works

IsdG and IsdI, Heme-degrading Enzymes in the Cytoplasm of Staphylococcus aureus

Skaar, E. P., Gaspar, A. H., & Schneewind, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307952200 · Cited by 282 · see citing works

ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12

Köster, W. L. (2001) · Research in Microbiology · doi:10.1016/s0923-2508(01)01200-1 · Cited by 277 · see citing works

Community-acquired methicillin-resistant Staphylococcus aureus: current perspectives

den Bergh, M. K.-V., & Kluytmans, J. A. J. W. (2006) · Clinical Microbiology and Infection · doi:10.1111/j.1469-0691.2006.01341.x · Cited by 244 · see citing works

Sideromycins: tools and antibiotics

Braun, V., Pramanik, A., Gwinner, T., Köberle, M., & Bohn, E. (2009) · BioMetals · doi:10.1007/s10534-008-9199-7 · Cited by 237 · see citing works

Role of Siderophore Biosynthesis in Virulence of <i>Staphylococcus aureus</i> : Identification and Characterization of Genes Involved in Production of a Siderophore

Dale, S. E., Doherty-Kirby, A., Lajoie, G., & Heinrichs, D. E. (2004) · Infection and Immunity · doi:10.1128/iai.72.1.29-37.2004 · Cited by 232 · see citing works

Staphylococcus aureus Redirects Central Metabolism to Increase Iron Availability

Friedman, D. B., Stauff, D. L., Pishchany, G., Whitwell, C. W., Torres, V. J., & Skaar, E. P. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020087 · Cited by 222 · see citing works

Pathogenesis of streptococcal and staphylococcal endocarditis

Moreillon, P., Que, Y., & Bayer, A. S. (2002) · Infectious Disease Clinics of North America · doi:10.1016/s0891-5520(01)00009-5 · Cited by 218 · see citing works

Haem recognition by a <i>Staphylococcus aureus</i> NEAT domain

Grigg, J. C., Vermeiren, C. L., Heinrichs, D. E., & Murphy, M. E. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05502.x · Cited by 166 · see citing works

Characterization of staphyloferrin A biosynthetic and transport mutants in <i>Staphylococcus aureus</i>

Beasley, F. C., Vinés, E. D., Grigg, J. C., Zheng, Q., Liu, S., Lajoie, G. A., Murphy, M. E. P., & Heinrichs, D. E. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06698.x · Cited by 163 · see citing works

Staphyloferrin A: a structurally new siderophore from staphylococci

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Identification of a novel iron regulated staphylococcal surface protein with haptoglobin‐haemoglobin binding activity

Dryla, A., Gelbmann, D., Von Gabain, A., & Nagy, E. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03542.x · Cited by 153 · see citing works

Staphylococcus aureus Transporters Hts, Sir, and Sst Capture Iron Liberated from Human Transferrin by Staphyloferrin A, Staphyloferrin B, and Catecholamine Stress Hormones, Respectively, and Contribute to Virulence

Beasley, F. C., Marolda, C. L., Cheung, J., Buac, S., & Heinrichs, D. E. (2011) · Infection and Immunity · doi:10.1128/iai.00117-11 · Cited by 151 · see citing works

Identification and Characterization of a Membrane Permease Involved in Iron-Hydroxamate Transport in <i>Staphylococcus aureus</i>

Sebulsky, M. T., Hohnstein, D., Hunter, M. D., & Heinrichs, D. E. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.16.4394-4400.2000 · Cited by 145 · see citing works

Molecular characterization of staphyloferrin B biosynthesis in <i>Staphylococcus aureus</i>

Cheung, J., Beasley, F. C., Liu, S., Lajoie, G. A., & Heinrichs, D. E. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06880.x · Cited by 144 · see citing works

Demonstration of the iron-regulated surface determinant (Isd) heme transfer pathway in Staphylococcus aureus

Muryoi, N., Tiedemann, M. T., Pluym, M., Cheung, J., Heinrichs, D. E., & Stillman, M. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802171200 · Cited by 144 · see citing works

Staphylococcus aureus IsdG and IsdI, Heme-degrading Enzymes with Structural Similarity to Monooxygenases

Wu, R., Skaar, E. P., Zhang, R., Joachimiak, G., Gornicki, P., Schneewind, O., & Joachimiak, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409526200 · Cited by 144 · see citing works

Quaternary Structure Regulates Hemin Dissociation from Human Hemoglobin

Hargrove, M. S., Whitaker, T. L., Olson, J. S., Vali, R. J., & Mathews, A. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.28.17385 · Cited by 143 · see citing works

Elucidation of the Mechanism by Which Catecholamine Stress Hormones Liberate Iron from the Innate Immune Defense Proteins Transferrin and Lactoferrin

Sandrini, S. M., Shergill, R., Woodward, J., Muralikuttan, R., Haigh, R. D., Lyte, M., & Freestone, P. P. (2010) · Journal of Bacteriology · doi:10.1128/jb.01028-09 · Cited by 143 · see citing works

Sortase Transpeptidases: Structural Biology and Catalytic Mechanism

Jacobitz, A. W., Kattke, M. D., Wereszczynski, J., & Clubb, R. (2017) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2017.04.008 · Cited by 143 · see citing works

The IsdG‐family of haem oxygenases degrades haem to a novel chromophore

Reniere, M. L., Ukpabi, G. N., Harry, S. R., Stec, D. F., Krull, R., Wright, D. W., Bachmann, B. O., Murphy, M. E., & Skaar, E. P. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07076.x · Cited by 139 · see citing works

NEAT: a domain duplicated in genes near the components of a putative Fe3+siderophore transporter from Gram-positive pathogenic bacteria

Andrade, M. A., Ciccarelli, F. D., Perez-Iratxeta, C., & Bork, P. (2002) · Genome Biology · doi:10.1186/gb-2002-3-9-research0047 · Cited by 135 · see citing works

Processing of Heme and Heme-Containing Proteins by Bacteria

Stojiljkovic, I., & Perkins-Balding, D. (2002) · DNA and Cell Biology · doi:10.1089/104454902753759708 · Cited by 134 · see citing works

Involvement of SirABC in Iron-Siderophore Import in <i>Staphylococcus aureus</i>

Dale, S. E., Sebulsky, M. T., & Heinrichs, D. E. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.24.8356-8362.2004 · Cited by 132 · see citing works

Identification and Characterization of fhuD1 and fhuD2 , Two Genes Involved in Iron-Hydroxamate Uptake in Staphylococcus aureus

Sebulsky, M. T., & Heinrichs, D. E. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.17.4994-5000.2001 · Cited by 130 · see citing works

Direct Hemin Transfer from IsdA to IsdC in the Iron-regulated Surface Determinant (Isd) Heme Acquisition System of Staphylococcus aureus

Liu, M., Tanaka, W. N., Zhu, H., Xie, G., Dooley, D. M., & Lei, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708372200 · Cited by 129 · see citing works

Trends in Invasive Methicillin-Resistant Staphylococcus aureus Infections

Iwamoto, M., Mu, Y., Lynfield, R., Bulens, S. N., Nadle, J., Aragon, D., Petit, S., Ray, S. M., Harrison, L. H., Dumyati, G. K., et al. (2013) · PEDIATRICS · doi:10.1542/peds.2013-1112 · Cited by 128 · see citing works

Pathway for Heme Uptake from Human Methemoglobin by the Iron-regulated Surface Determinants System of Staphylococcus aureus

Zhu, H., Xie, G., Liu, M., Olson, J. S., Fabian, M., Dooley, D. M., & Lei, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801466200 · Cited by 127 · see citing works

Biosynthetic Analysis of the Petrobactin Siderophore Pathway from Bacillusanthracis

Lee, J. Y., Janes, B. K., Passalacqua, K. D., Pfleger, B. F., Bergman, N. H., Liu, H., Håkansson, K., Somu, R. V., Aldrich, C. C., Cendrowski, S. R., et al. (2006) · Journal of Bacteriology · doi:10.1128/jb.01526-06 · Cited by 123 · see citing works

Molecular characterization of the ferric-uptake regulator, Fur, from Staphylococcus aureus The GenBank accession numbers for the S. aureus fur gene and fhu operon reported in this paper are AF118839 and AF132117, respectively.

Xiong, A., Singh, V. K., Cabrera, G., & Jayaswal, R. K. (2000) · Microbiology · doi:10.1099/00221287-146-3-659 · Cited by 122 · see citing works

Crystal Structure of the Heme-IsdC Complex, the Central Conduit of the Isd Iron/Heme Uptake System in Staphylococcus aureus

Sharp, K. H., Schneider, S., Cockayne, A., & Paoli, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700234200 · Cited by 120 · see citing works

Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin

Pilpa, R. M., Robson, S. A., Villareal, V. A., Wong, M. L., Phillips, M., & Clubb, R. T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806007200 · Cited by 118 · see citing works

Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus

Lee, W. C., Reniere, M. L., Skaar, E. P., & Murphy, M. E. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709486200 · Cited by 117 · see citing works

Transferrin binding in Staphylococcus aureus: involvement of a cell wall‐anchored protein

Taylor, J. M., & Heinrichs, D. E. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02850.x · Cited by 116 · see citing works

The Ferrichrome Uptake Pathway inPseudomonas aeruginosaInvolves an Iron Release Mechanism with Acylation of the Siderophore and Recycling of the Modified Desferrichrome

Hannauer, M., Barda, Y., Mislin, G. L. A., Shanzer, A., & Schalk, I. J. (2010) · Journal of Bacteriology · doi:10.1128/jb.01539-09 · Cited by 114 · see citing works

Purification and chemical characterization of staphyloferrin B, a hydrophilic siderophore from staphylococci

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Coordination chemistry of microbial iron transport compounds. 24. Characterization of coprogen and ferricrocin, two ferric hydroxamate siderophores

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Management of common bacterial infections of the skin

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The hemolysins of Staphylococcus aureus

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Coordination Chemistry of the Carboxylate Type Siderophore Rhizoferrin: The Iron(III) Complex and Its Metal Analogs

Carrano, C. J., Drechsel, H., Kaiser, D., Jung, G., Matzanke, B. F., Winkelmann, G., Rochel, N., & Albrecht-Gary, A. M. (1996) · Inorganic Chemistry · doi:10.1021/ic960526d · Cited by 101 · see citing works

Molecular Cloning and Analysis of a Putative Siderophore ABC Transporter from Staphylococcus aureus

Morrissey, J. A., Cockayne, A., Hill, P. J., & Williams, P. M. (2000) · Infection and Immunity · doi:10.1128/iai.68.11.6281-6288.2000 · Cited by 98 · see citing works

Staphylococcal Vaccines and Immunotherapies

Schaffer, A. C., & Lee, J. C. (2009) · Infectious Disease Clinics of North America · doi:10.1016/j.idc.2008.10.005 · Cited by 97 · see citing works

Heme Coordination by Staphylococcus aureus IsdE

Grigg, J. C., Vermeiren, C. L., Heinrichs, D. E., & Murphy, M. E. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704602200 · Cited by 96 · see citing works

Isolation and biological characterization of staphyloferrin B, a compound with siderophore activity from staphylococci

Haag, H., Fiedler, H., Meiwes, J., Drechsel, H., Jung, G., & Zähner, H. (1994) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1994.tb06626.x · Cited by 96 · see citing works

Baulamycins A and B, Broad-Spectrum Antibiotics Identified as Inhibitors of Siderophore Biosynthesis in Staphylococcus aureus and Bacillus anthracis

Tripathi, A., Schofield, M. M., Chlipala, G. E., Schultz, P. J., Yim, I., Newmister, S. A., Nusca, T. D., Scaglione, J. B., Hanna, P. C., Tamayo‐Castillo, G., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja4115924 · Cited by 96 · see citing works

Identification and Characterization of the <i>Staphylococcus aureus</i> Gene Cluster Coding for Staphyloferrin A

Cotton, J. L., Tao, J., & Balibar, C. J. (2009) · Biochemistry · doi:10.1021/bi801844c · Cited by 95 · see citing works

Requirement of <i>Staphylococcus aureus</i> ATP-Binding Cassette-ATPase FhuC for Iron-Restricted Growth and Evidence that It Functions with More than One Iron Transporter

Speziali, C. D., Dale, S. E., Henderson, J. A., Vinés, E. D., & Heinrichs, D. E. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.6.2048-2055.2006 · Cited by 95 · see citing works

Unique Heme-Iron Coordination by the Hemoglobin Receptor IsdB of Staphylococcus aureus

Gaudin, C. F. M., Grigg, J. C., Arrieta, A. L., & Murphy, M. E. P. (2011) · Biochemistry · doi:10.1021/bi200369p · Cited by 93 · see citing works

Solution Structure of the NEAT (NEAr Transporter) Domain from IsdH/HarA: the Human Hemoglobin Receptor in Staphylococcus aureus

Pilpa, R. M., Fadeev, E. A., Villareal, V. A., Wong, M. L., Phillips, M. L., & Clubb, R. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.019 · Cited by 92 · see citing works

Siderophore-mediated iron acquisition in the staphylococci

Beasley, F. C., & Heinrichs, D. E. (2010) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2009.09.011 · Cited by 90 · see citing works

Heme Degradation by Staphylococcus aureus IsdG and IsdI Liberates Formaldehyde Rather Than Carbon Monoxide

Matsui, T., Nambu, S., Ono, Y., Goulding, C. W., Tsumoto, K., & Ikeda‐Saito, M. (2013) · Biochemistry · doi:10.1021/bi400382p · Cited by 90 · see citing works

The Role of FhuD2 in Iron(III)-Hydroxamate Transport in Staphylococcus aureus

Sebulsky, M. T., Shilton, B. H., Speziali, C. D., & Heinrichs, D. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305073200 · Cited by 90 · see citing works

Coordination isomers of biological iron transport compounds. V. The preparation and chirality of the chromium(III) enterobactin complex and model tris(catechol)chromium(III) analogues

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Synthesis of L-2,3-Diaminopropionic Acid, a Siderophore and Antibiotic Precursor

Kobylarz, M. J., Grigg, J. C., Takayama, S.-I. J., Rai, D. K., Heinrichs, D. E., & Murphy, M. E. P. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.12.011 · Cited by 88 · see citing works

IsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus

Pishchany, G., Sheldon, J. R., Dickson, C. F., Alam, M. T., Read, T. D., Gell, D. A., Heinrichs, D. E., & Skaar, E. P. (2014) · The Journal of Infectious Diseases · doi:10.1093/infdis/jit817 · Cited by 88 · see citing works

The Effect of Growth Conditions on Oxidative and Dehydrogenase Activity in Staphylococcus aureus

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Structural Basis for Multimeric Heme Complexation through a Specific Protein-Heme Interaction

Watanabe, M., Tanaka, Y., Suenaga, A., Kuroda, M., Yao, M., Watanabe, N., Arisaka, F., Ohta, T., Tanaka, I., & Tsumoto, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803383200 · Cited by 83 · see citing works

Staphyloferrin A as siderophore-component in fluoroquinolone-based Trojan horse antibiotics

Milner, S. J., Seve, A., Snelling, A. M., Thomas, G. H., Kerr, K. G., Routledge, A., & Duhme‐Klair, A. (2013) · Organic & Biomolecular Chemistry · doi:10.1039/c3ob40162f · Cited by 77 · see citing works

Characterization and Analysis of Early Enzymes for Petrobactin Biosynthesis in Bacillus anthracis

Pfleger, B. F., Lee, J. Y., Somu, R. V., Aldrich, C. C., Hanna, P. C., & Sherman, D. H. (2007) · Biochemistry · doi:10.1021/bi6023995 · Cited by 75 · see citing works

The Staphylococcus aureus Siderophore Receptor HtsA Undergoes Localized Conformational Changes to Enclose Staphyloferrin A in an Arginine-rich Binding Pocket

Grigg, J. C., Cooper, J. D., Cheung, J., Heinrichs, D. E., & Murphy, M. E. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.097865 · Cited by 75 · see citing works

FhuD1, a Ferric Hydroxamate-binding Lipoprotein in Staphylococcus aureus

Sebulsky, M. T., Speziali, C. D., Shilton, B. H., Edgell, D. R., & Heinrichs, D. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409793200 · Cited by 75 · see citing works

High-Affinity Binding of the Staphylococcal HarA Protein to Haptoglobin and Hemoglobin Involves a Domain with an Antiparallel Eight-Stranded β-Barrel Fold

Dryla, A., Hoffmann, B., Gelbmann, D., Giefing, C., Hanner, M., Meinke, A., Anderson, A. S., Koppensteiner, W., Konrat, R., von Gabain, A., et al. (2007) · Journal of Bacteriology · doi:10.1128/jb.01366-06 · Cited by 73 · see citing works

Identification and Characterization of SirA, an Iron-Regulated Protein from Staphylococcus aureus

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Specificity of Staphyloferrin B Recognition by the SirA Receptor from Staphylococcus aureus

Grigg, J. C., Cheung, J., Heinrichs, D. E., & Murphy, M. E. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172924 · Cited by 71 · see citing works

Proteins of the penicillin biosynthesis pathway

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Iron Transport in Escherichia coli : Uptake and Modification of Ferrichrome

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Transcriptional modulation of some Staphylococcus aureus iron-regulated genes during growth in vitro and in a tissue cage model in vivo

Allard, M., Moisan, H., Brouillette, É., Gervais, A. L., Jacques, M., Lacasse, P., Diarra, M. S., & Malouin, F. (2006) · Microbes and Infection · doi:10.1016/j.micinf.2006.01.022 · Cited by 67 · see citing works

Nasal Carriage of Staphylococcus aureus in Botucatu, Brazil: A Population-Based Survey

Pires, F. V., da Cunha, M. D. L. R. D. S., Abraão, L. M., Faccioli-Martins, P. Y., Camargo, C. H., & Fortaleza, C. M. C. B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092537 · Cited by 66 · see citing works

Transient Weak Protein–Protein Complexes Transfer Heme Across the Cell Wall of Staphylococcus aureus

Villareal, V. A., Spirig, T., Robson, S. A., Liu, M., Lei, B., & Clubb, R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203805b · Cited by 63 · see citing works

<scp>TCA</scp> cycle activity in <scp> <i>S</i> </scp> <i>taphylococcus aureus</i> is essential for iron‐regulated synthesis of staphyloferrin <scp>A</scp> , but not staphyloferrin <scp>B</scp> : the benefit of a second citrate synthase

Sheldon, J. R., Marolda, C. L., & Heinrichs, D. E. (2014) · Molecular Microbiology · doi:10.1111/mmi.12593 · Cited by 62 · see citing works

Iron-Coordinating Tyrosine Is a Key Determinant of NEAT Domain Heme Transfer

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Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI

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