A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry
Author:
Affiliation:
1. Department of Chemistry Pomona College Claremont CA USA
2. Department of Wine Studies Santa Rosa Junior College CA USA
3. Department of Biology Pomona College Claremont CA USA
Publisher
Wiley
Subject
General Biochemistry, Genetics and Molecular Biology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/2211-5463.12439
Reference23 articles.
1. Determination of coenzyme A levels inPyrococcus furiosusand other Archaea: implications for a general role for coenzyme A in thermophiles
2. Insights into the Metabolism of Elemental Sulfur by the Hyperthermophilic Archaeon Pyrococcus furiosus : Characterization of a Coenzyme A- Dependent NAD(P)H Sulfur Oxidoreductase
3. DNA Microarray Analysis of the Hyperthermophilic Archaeon Pyrococcus furiosus : Evidence for a New Type of Sulfur-Reducing Enzyme Complex
4. Structure and Substrate Specificity of the Pyrococcal Coenzyme A Disulfide Reductases/Polysulfide Reductases (CoADR/Psr): Implications for S0-Based Respiration and a Sulfur-Dependent Antioxidant System in Pyrococcus
5. Pyridine Nucleotide Complexes with Bacillus anthracis Coenzyme A-Disulfide Reductase: A Structural Analysis of Dual NAD(P)H Specificity
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