Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

M.H. Sazinsky; M. Merkx; E. Cadieux; Sonya Tang; S.J. Lippard

doi:10.1021/bi048140z

Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

M.H. Sazinsky
, M. Merkx
, E. Cadieux
, Sonya Tang
, S.J. Lippard

Research output: Contribution to journal › Article › Academic › peer-review

43 Citations (Scopus)

1 Downloads (Pure)

Abstract

A three-component soluble methane monooxygenase (sMMO) enzyme system catalyzes the hydroxylation of methane to methanol at a carboxylate-bridged diiron center housed in the a-subunit of the hydroxylase (MMOH). Catalysis is facilitated by the presence of a regulatory protein (MMOB) and inhibited by MMOD, a protein of unknown function encoded in the sMMO operon. Both MMOB and MMOD are presumed to bind to the same region of the MMOH a-subunit. A colorimetric method for monitoring removal of Fe(II) from MMOH was developed using 1,10-phenanthroline and yields apo MMOH with

Original language	English
Pages (from-to)	16263-16276
Journal	Biochemistry
Volume	43
Issue number	51
DOIs	https://doi.org/10.1021/bi048140z
Publication status	Published - 2004

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title = "Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)",

abstract = "A three-component soluble methane monooxygenase (sMMO) enzyme system catalyzes the hydroxylation of methane to methanol at a carboxylate-bridged diiron center housed in the a-subunit of the hydroxylase (MMOH). Catalysis is facilitated by the presence of a regulatory protein (MMOB) and inhibited by MMOD, a protein of unknown function encoded in the sMMO operon. Both MMOB and MMOD are presumed to bind to the same region of the MMOH a-subunit. A colorimetric method for monitoring removal of Fe(II) from MMOH was developed using 1,10-phenanthroline and yields apo MMOH with",

author = "M.H. Sazinsky and M. Merkx and E. Cadieux and Sonya Tang and S.J. Lippard",

year = "2004",

doi = "10.1021/bi048140z",

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volume = "43",

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journal = "Biochemistry",

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publisher = "American Chemical Society",

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TY - JOUR

T1 - Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

AU - Sazinsky, M.H.

AU - Merkx, M.

AU - Cadieux, E.

AU - Tang, Sonya

AU - Lippard, S.J.

PY - 2004

Y1 - 2004

N2 - A three-component soluble methane monooxygenase (sMMO) enzyme system catalyzes the hydroxylation of methane to methanol at a carboxylate-bridged diiron center housed in the a-subunit of the hydroxylase (MMOH). Catalysis is facilitated by the presence of a regulatory protein (MMOB) and inhibited by MMOD, a protein of unknown function encoded in the sMMO operon. Both MMOB and MMOD are presumed to bind to the same region of the MMOH a-subunit. A colorimetric method for monitoring removal of Fe(II) from MMOH was developed using 1,10-phenanthroline and yields apo MMOH with

AB - A three-component soluble methane monooxygenase (sMMO) enzyme system catalyzes the hydroxylation of methane to methanol at a carboxylate-bridged diiron center housed in the a-subunit of the hydroxylase (MMOH). Catalysis is facilitated by the presence of a regulatory protein (MMOB) and inhibited by MMOD, a protein of unknown function encoded in the sMMO operon. Both MMOB and MMOD are presumed to bind to the same region of the MMOH a-subunit. A colorimetric method for monitoring removal of Fe(II) from MMOH was developed using 1,10-phenanthroline and yields apo MMOH with

U2 - 10.1021/bi048140z

DO - 10.1021/bi048140z

M3 - Article

C2 - 15610020

SN - 0006-2960

VL - 43

SP - 16263

EP - 16276

JO - Biochemistry

JF - Biochemistry

IS - 51

ER -

Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

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