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

Journal Article · Wed Mar 02 00:00:00 EST 1988 · J. Am. Chem. Soc.; (United States)

DOI:https://doi.org/10.1021/ja00213a059· OSTI ID:7247353

Shiemke, A K; Scott, R A; Shelnutt, J A

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), Vol. 110:5
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
NICKEL COMPLEXES
STRUCTURAL CHEMICAL ANALYSIS
OXIDOREDUCTASES
SULFONIC ACIDS
EXPERIMENTAL DATA
RAMAN SPECTROSCOPY
RESONANCE SCATTERING
COMPLEXES
DATA
ENZYMES
INELASTIC SCATTERING
INFORMATION
LASER SPECTROSCOPY
NUMERICAL DATA
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
SCATTERING
SPECTROSCOPY
TRANSITION ELEMENT COMPLEXES
400201* - Chemical & Physicochemical Properties