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Investigation by EPR and ENDOR spectroscopy of the nickel(I) form of cofactor F{sub 430} of Methanobacterium thermoautorophicum and of nickel(I) octaethylisobacteriochlorin

Journal Article · · Journal of the American Chemical Society
DOI:https://doi.org/10.1021/ja9625337· OSTI ID:458612
; ;  [1]; ;  [2]; ; ;  [3]
  1. Northwestern Univ., Evanston, IL (United States)
  2. Brookhaven National Lab., Upton, NY (United States)
  3. Univ. of Georgia, Athens, GA (United States)

The terminal step in methane generation by the archaeon Methanobacterium thermoautotrophicum is catalyzed by the enzyme S-methyl coenzyme M reductase (methylreductase). This enzyme contains a Ni(II) tetrapyrrole cofactor, F{sub 430}, at the active site in the resting state. A Ni(I) state (Ni{sup I}F{sub 430}) has been proposed as the active form of the cofactor. Nickel isobacteriochlorins have been used to model F{sub 430}. We have investigated both Ni{sup I}F{sub 430} and Ni{sup I}OEiBC using CW and pulsed EPR and ENDOR spectroscopy at X-band and Q-band microwave frequencies. In agreement with a previous X-band EPR and ESEEM study, at Q-band, the g tensor of Ni{sup I}F{sub 430} appears axial and {sup 1,2}H ENDOR of Ni{sup I}F{sub 430} in H{sub 2}O versus D{sub 2}O solvent shows no evidence for strongly coupled, solvent-exchangeable hydrogens, and this indicates that there is no water axially coordinated to Ni(I) in contrast to the Ni(II) resting state. Both Ni{sup I}F{sub 430} and Ni{sup I}OEiBC give {sup 14}N ENDOR signals arising from the four pyrrole nitrogen ligands to Ni(I). Previous EXAFS studies of Ni{sup I}OEiBC and Ni{sup I}F{sub 430}Me{sub 5} showed two sets of Ni(I)-N distances differing by nearly 8%, and in agreement with this, the {sup 14}N ENDOR signals for both Ni{sup I}OEiBC and Ni{sup I}F{sub 430} can be analyzed in terms of superimposed signals from two distinct types of nitrogen ligand. 86 refs., 5 figs., 3 tabs.

Research Organization:
Brookhaven National Laboratory (BNL), Upton, NY
DOE Contract Number:
AC02-76CH00016
OSTI ID:
458612
Journal Information:
Journal of the American Chemical Society, Journal Name: Journal of the American Chemical Society Journal Issue: 4 Vol. 119; ISSN JACSAT; ISSN 0002-7863
Country of Publication:
United States
Language:
English

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