Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 15, Issue 2, Pages 319-327Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2011.02.012
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Funding
- AFOSR Multidisciplinary University Research Initiative [FA9550-05-01-0365]
- Department of Energy Office of Basic Energy Sciences [DE-FG02-10ER16194]
- NASA Astrobiology Institute (NAI)-Funded Astrobiology Biogeocatalysis Research Center [NNA08C-N85A]
- NAI
- Department of Energy, Office of Biological and Environmental Research
- National Institutes of Health, National Center for Research Resources, Biomedical Technology
- National Institute of General Medical Sciences
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Recent advances in our understanding of the mechanisms for the biosynthesis of the complex iron-sulfur (Fe-S) containing prosthetic groups associated with [FeFe]-hydrogenases and nitrogenases have revealed interesting parallels. The biosynthesis,of the H-cluster ([FeFe]-hydrogenase) and the FeMo-co (nitrogenase) occurs through a coordinated process that involves the modification of Fe-S cluster precursors synthesized by the general host cell machinery (lsc/Suf). Key modifications to the Fe-S precursors are introduced by the activity of radical S-adenosylmethionine (SAM) enzymes on unique scaffold proteins. The transfer of the modified clusters to a cofactor-less structural apo-protein completes maturation. Together these features provide the basis for establishing unifying paradigms for complex Fe-S cluster biosynthesis for these enzymes.
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