Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase.

Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase. Research Abstract Details 

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Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase. Abstract Text:

W Anthony Oertling,Charisa D Cornellison,Nathan R Treff,Junji Watanabe,Michelle A Pressler,Jeanne R Small,

We report a protein conformational change following carbon monoxide photodetachment from fully reduced bovine cytochrome c oxidase that is hypothesized to be associated with changes in ligand mobility through a dioxygen access channel in the protein. Although not resolved by earlier photoacoustic or optical studies on this adduct, utilization of slightly lower temperatures revealed a process with a kinetic lifetime of about 70 ns at 10 degrees C. We measure an enthalpy change of about 8 kcal/mol in 0.050 M HEPES buffer that becomes less endothermic (DeltaH approximately 2 kcal/mol) at higher ionic strength. The volume contraction of about -0.7 mL/mol associated with the process almost doubles in higher ionic strength buffer systems. Measurements of samples in phosphate buffer systems are similar and appear to display the same subtle ionic strength dependence. Both the isolation of this photoacoustic signal component and the possible dependence on ionic strength of the thermodynamic parameters derived from its analysis appear analogous to and consistent with prior photoacoustic results monitoring CO photodetachment from the camphor complex of cytochrome P-450. Accordingly, we consider a similar model in which a conformational change results in movement of an exposed charged group or groups towards the interior of the protein, out of contact with solvent, as in the closing of a salt bridge.

Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase. Publishing Authors By Initials

WA Oertling,CD Cornellison,NR Treff,J Watanabe,MA Pressler,JR Small,

For similar natural sciences: physics: thermodynamics research abstracts see: natural sciences: physics: thermodynamics research

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Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of inorganic biochemistry

VOLUME: 101

Page Numbers: 635-43

Journal Abbreviation: J. Inorg. Biochem.

ISSN: 0162-0134

DAY: 21

MONTH: 12

YEAR: 2006

Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase. Information

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LANGUAGE: eng

NlmUniqueID: 7905788

Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase. Keywords Mesh Terms:

KEYWORDS: Thermodynamics

MESH TERMS: chemistry

Chemical & Substance for Abstract: Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase. Information

Substance Name: Electron Transport Complex IV

Registry Number: EC 1.9.3.1

Grant and Affiliation Information for Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase.

AFFILIATION: Department of Chemistry and Biochemistry, 226 Science Building, Eastern Washington University, Cheney, WA 99004-2440, USA. WOertling@ewu.edu

Country: United States

AGENCY: United States NIGMS

GRANT: R44-GM51147

ACRONYM: GM

MEDLINETA: J Inorg Biochem

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