Incorporation of either molybdenum or tungsten into formate dehydrogenase from Desulfovibrio alaskensis NCIMB 13491; EPR assignment of the proximal iron-sulfur cluster to the pterin cofactor in formate dehydrogenases from sulfate-reducing bacteria
Open Access
- 11 December 2003
- journal article
- research article
- Published by Springer Nature in JBIC Journal of Biological Inorganic Chemistry
- Vol. 9 (2) , 145-151
- https://doi.org/10.1007/s00775-003-0506-z
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Two W‐containing formate dehydrogenases (CO2‐reductases) involved in syntrophic propionate oxidation by Syntrophobacter fumaroxidansEuropean Journal of Biochemistry, 2003
- Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigasStructure, 2002
- Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site 1 1Edited by P. E. WrightJournal of Molecular Biology, 2000
- Observation of Ligand-Based Redox Chemistry at the Active Site of a Molybdenum EnzymeJournal of the American Chemical Society, 1999
- The high resolution crystal structure of DMSO reductase in complex with DMSO 1 1Edited by D. C. ReesJournal of Molecular Biology, 1998
- Structure and function of molybdopterin containing enzymesProgress in Biophysics and Molecular Biology, 1997
- Crystal Structure of Dimethyl Sulfoxide Reductase fromRhodobacter capsulatusat 1.88 Å ResolutionJournal of Molecular Biology, 1996
- Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin CoordinationScience, 1996
- Using saturation-recovery EPR to measure exchange couplings in proteins: application to ribonucleotide reductaseJournal of the American Chemical Society, 1992
- Electron paramagnetic resonance studies of the tungsten-containing formate dehydrogenase fromBiochemical and Biophysical Research Communications, 1987