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Resonance Raman spectroscopic investigation of axial coordination in M. thermoautotrophicum methyl reductase and its nickel tetrapyrrole cofactor F/sub 430/ave

Journal Article · · J. Am. Chem. Soc.; (United States)
DOI:https://doi.org/10.1021/ja00213a059· OSTI ID:7247353

The S-methyl coenzyme M (CH/sub 3/-S-CoM, 2-(methylthio)ethanesulfonic acid) methylreductase enzyme of Methanobacterium thermoautotrophicum contains F/sub 430/, the nickel-tetrapyrrole cofactor which is thought to be the site of reduction of CH/sub 3/-S-CoM to methane and HS-CoM. Here the use of resonance Raman spectroscopy is reported for the investigation of the well-characterized forms of isolated F/sub 430/ in aqueous solution and the intact methylreductase. The Raman spectra were obtained on pairs of 100-200 ..mu..M samples by using a split cell designed for a Raman difference spectrometer described previously. The spectra were excited at 441.6 nm with a 40 mW defocused, unpolarized beam of a helium-cadmium laser (Omnichrome) operating at 4-cm/sup -1/ resolution.

Research Organization:
Univ. of Georgia, Athens (USA)
DOE Contract Number:
AC04-76DP00789
OSTI ID:
7247353
Journal Information:
J. Am. Chem. Soc.; (United States), Journal Name: J. Am. Chem. Soc.; (United States) Vol. 110:5; ISSN JACSA
Country of Publication:
United States
Language:
English