The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductase.

Abstract:

:Methane monooxygenase (MMO) catalyses the biological transformation of methane to methanol at a binuclear iron site. Guided by the three-dimensional structure of the R2 protein of E. coli ribonucleotide reductase (RNR), we have aligned the sequences of two different MMOs with the sequences of the iron coordinating four helix bundle in R2. The model suggests that the central four helix bundle of R2 is present also in MMO. The iron coordination is similar in MMO and R2 with two histidine ligands and four carboxyl ligands in both cases. The residues lining the proposed oxygen binding site in MMO are significantly smaller in MMO than in R2 allowing binding of both molecular oxygen and methane at this site. This binding site is lined by residues Cys151, Thr213, Ile217 and Ile(Val)239.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Nordlund P,Dalton H,Eklund H

doi

10.1016/0014-5793(92)80690-i

keywords:

subject

Has Abstract

pub_date

1992-08-03 00:00:00

pages

257-62

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80690-I

journal_volume

307

pub_type

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