Plausible structure of the iron-molybdenum cofactor of nitrogenase.
A plausible structure of the iron-molybdenum cofactor of nitrogenase [reduced ferredoxin:dinitrogen oxidoreductase (ATP-hydrolyzing), EC 1.18.6.1] is presented based on altered substrate reduction properties of dinitrogenase containing homocitrate analogs within the cofactor. Alterations on each carbon of the four-carbon homocitrate backbone were correlated with altered substrate reduction properties of dinitrogenase containing these analogs. Altered substrate reduction properties are the basis for a model in which homocitrate is oriented about two cubane metal clusters.
Madden
M S
MS
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.
Krezel
A M
AM
Allen
R M
RM
Ludden
P W
PW
Shah
V K
VK
D005561:Formates / Q000737:chemistry; D066298:In Vitro Techniques; D015394:Molecular Structure; D008983:Molybdoferredoxin / Q000648:ultrastructure*; D009591:Nitrogenase / Q000378:metabolism / Q000648:ultrastructure*; D010084:Oxidation-Reduction; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D014233:Tricarboxylic Acids / Q000737:chemistry
D005561:Formates; D008983:Molybdoferredoxin; D014233:Tricarboxylic Acids; C028143:homocitric acid; D009591:Nitrogenase