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| [[Image:2nvf.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2nvf| PDB=2nvf | SCENE= }} | | {{STRUCTURE_2nvf| PDB=2nvf | SCENE= }} |
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| '''Soluble domain of Rieske Iron-Sulfur protein.'''
| | ===Soluble domain of Rieske Iron-Sulfur protein.=== |
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| ==Overview==
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| The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc(1) functions as the initial electron acceptor in the rate-limiting step of the catalytic reaction. Prior studies have established roles for a number of conserved residues that hydrogen bond to ligands of the [2Fe-2S] cluster. We have constructed site-specific variants at two of these residues, measured their thermodynamic and functional properties, and determined atomic resolution X-ray crystal structures for the native protein at 1.2 A resolution and for five variants (Ser-154-->Ala, Ser-154-->Thr, Ser-154-->Cys, Tyr-156-->Phe, and Tyr-156-->Trp) to resolutions between 1.5 A and 1.1 A. These structures and complementary biophysical data provide a molecular framework for understanding the role hydrogen bonds to the cluster play in tuning thermodynamic properties, and hence the rate of this bioenergetic reaction. These studies provide a detailed structure-function dissection of the role of hydrogen bonds in tuning the redox potentials of [2Fe-2S] clusters. | | The line below this paragraph, {{ABSTRACT_PUBMED_17223530}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17223530 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17223530}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lhee, S.]] | | [[Category: Lhee, S.]] |
| [[Category: Nair, S K.]] | | [[Category: Nair, S K.]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:57:26 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:29:43 2008'' |
