Resonance Raman spectroscopic investigation of axial coordination in M. thermoautotrophicum methyl reductase and its nickel tetrapyrrole cofactor F/sub 430/ave
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
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Related Subjects
400201* -- Chemical & Physicochemical Properties
COMPLEXES
DATA
ENZYMES
EXPERIMENTAL DATA
INELASTIC SCATTERING
INFORMATION
LASER SPECTROSCOPY
NICKEL COMPLEXES
NUMERICAL DATA
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
OXIDOREDUCTASES
RAMAN SPECTROSCOPY
RESONANCE SCATTERING
SCATTERING
SPECTROSCOPY
STRUCTURAL CHEMICAL ANALYSIS
SULFONIC ACIDS
TRANSITION ELEMENT COMPLEXES