Substrate reduction properties of dinitrogenase activated in vitro are dependent upon the presence of homocitrate or its analogs during iron-molybdenum cofactor synthesis
- 19 September 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (19) , 7796-7799
- https://doi.org/10.1021/bi00445a040
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 6 references indexed in Scilit:
- Homocitrate is a component of the iron-molybdenum cofactor of nitrogenaseBiochemistry, 1989
- Dinitrogenase with altered substrate specificity results from the use of homocitrate analogs for in vitro synthesis of the iron-molybdenum cofactorBiochemistry, 1988
- Iron-molybdenum cofactor biosynthesis in Azotobacter vinelandii requires the iron protein of nitrogenase.Journal of Biological Chemistry, 1987
- nifV-dependent, low-molecular-weight factor required for in vitro synthesis of iron-molybdenum cofactor of nitrogenaseJournal of Bacteriology, 1986
- In vitro synthesis of the iron-molybdenum cofactor of nitrogenase.Proceedings of the National Academy of Sciences, 1986
- Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle.Proceedings of the National Academy of Sciences, 1978