Electron paramagnetic resonance studies of 95Mo-enriched NADH dehydrogenase isolated from iron-deficient Azotobacter vinelandii
- 16 December 1970
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Enzymology
- Vol. 220 (3) , 443-448
- https://doi.org/10.1016/0005-2744(70)90275-5
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Isolation by crystallization of the MoFe protein of Azotobacter nitrogenaseBiochemical and Biophysical Research Communications, 1970
- Paramagnetic monomeric molybdenum(V)-cysteine complex as a model for molybdenum-enzyme interactionJournal of the American Chemical Society, 1970
- Purification and properties of two iron-sulfur proteins from Azotobacter vinelandiiBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- The cytochrome system of Azotobacter vinelandiiBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1967
- Purification, metal composition and properties of molybdo-ferredoxin and azoferredoxin, two of the components of the nitrogen-fixing system of Clostridium pasteurianumBiochimica et Biophysica Acta (BBA) - General Subjects, 1967
- Identification of sulfur as component of the EPR signal at g = 1.94 by isotopic substitutionBiochemical and Biophysical Research Communications, 1967
- Resolution of complex I (DPNH-coenzyme Q reductase) of the mitochondrial electron transfer systemBiochemical and Biophysical Research Communications, 1967
- Electron Spin Resonance of Xanthine Oxidase Substituted with Molybdenum-95Nature, 1966
- Molybdenum–Thiol Complexes as Models for Molybdenum Bound in EnzymesNature, 1966
- A Superhyperfine Interaction Involving 33S in the Iron-containing Proteins of Azotobacter vinelandiiJournal of Biological Chemistry, 1966