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1fz2

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[[Image:1fz2.gif|left|200px]]
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{{STRUCTURE_1fz2| PDB=1fz2 | SCENE= }}
{{STRUCTURE_1fz2| PDB=1fz2 | SCENE= }}
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'''METHANE MONOOXYGENASE HYDROXYLASE, FORM II MIXED-VALENT GENERATED BY CRYSTAL SOAKING'''
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===METHANE MONOOXYGENASE HYDROXYLASE, FORM II MIXED-VALENT GENERATED BY CRYSTAL SOAKING===
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==Overview==
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The oxidation of methane to methanol is performed at carboxylate-bridged dinuclear iron centers in the soluble methane monooxygenase hydroxylase (MMOH). Previous structural studies of MMOH, and the related R2 subunit of ribonucleotide reductase, have demonstrated the occurrence of carboxylate shifts involving glutamate residues that ligate the catalytic iron atoms. These shifts are thought to have important mechanistic implications. Recent kinetic and theoretical studies have also emphasized the importance of hydrogen bonding and pH effects at the active site. We report here crystal structures of MMOH from Methylococcus capsulatus (Bath) in the diiron(II), diiron(III), and mixed-valent Fe(II)Fe(III) oxidation states, and at pH values of 6.2, 7.0, and 8.5. These structures were investigated in an effort to delineate the range of possible motions at the MMOH active site and to identify hydrogen-bonding interactions that may be important in understanding catalysis by the enzyme. Our results present the first view of the diiron center in the mixed-valent state, and they indicate an increased lability for ferrous ions in the enzyme. Alternate conformations of Asn214 near the active site according to redox state and a distortion in one of the alpha-helices adjacent to the metal center in the diiron(II) state have also been identified. These changes alter the surface of the protein in the vicinity of the catalytic core and may have implications for small-molecule accessibility to the active site and for protein component interactions in the methane monooxygenase system. Collectively, these results help to explain previous spectroscopic observations and provide new insight into catalysis by the enzyme.
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The line below this paragraph, {{ABSTRACT_PUBMED_11456616}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11456616 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11456616}}
==About this Structure==
==About this Structure==
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[[Category: Dinuclear iron center]]
[[Category: Dinuclear iron center]]
[[Category: Monooxygenase]]
[[Category: Monooxygenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:55:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:09:20 2008''

Revision as of 01:09, 1 July 2008

Image:1fz2.png

Template:STRUCTURE 1fz2

METHANE MONOOXYGENASE HYDROXYLASE, FORM II MIXED-VALENT GENERATED BY CRYSTAL SOAKING

Template:ABSTRACT PUBMED 11456616

About this Structure

1FZ2 is a Protein complex structure of sequences from Methylococcus capsulatus. Full crystallographic information is available from OCA.

Reference

Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site., Whittington DA, Lippard SJ, J Am Chem Soc. 2001 Feb 7;123(5):827-38. PMID:11456616

Page seeded by OCA on Tue Jul 1 04:09:20 2008

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