X-ray Absorption and Resonance Raman Studies of Methyl-Coenzyme M Reductase Indicating That Ligand Exchange and Macrocycle Reduction Accompany Reductive Activation-Reference-Cited by-同舟云学术

X-ray Absorption and Resonance Raman Studies of Methyl-Coenzyme M Reductase Indicating That Ligand Exchange and Macrocycle Reduction Accompany Reductive Activation

Published:2002-10-12 Issue:44 Volume:124 Page:13242-13256
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Tang Qun¹,Carrington Paul E.¹,Horng Yih-Chern¹,Maroney Michael J.¹,Ragsdale Stephen W.¹,Bocian David F.¹

Affiliation:

1. Contribution from the Department of Chemistry, University of California, Riverside, California 92521-0403, Department of Chemistry, University of Massachusetts, Amherst, Massachusetts, and Department of Biochemistry, Beadle Center, University of Nebraska, Lincoln, Nebraska 68588-0664

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja020314h

Reference49 articles.

1. UNUSUAL COENZYMES OF METHANOGENESIS

2. On the role ofN-7-mercaptoheptanoyl-O-phospho-L-threonine (component B) in the enzymatic reduction of methyl-coenzyme M to methane

3. Nickel, a component of factor F 430 from Methanobacterium thermoautotrophicum

4. Biosynthetic evidence for a nickel tetrapyrrole structure of factor F430 from Methanobacterium thermoautotrophicum

5. Presence of nickel in Factor F430 from Methanobacteriumbryantii

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