Direct measurement of proton release by cytochrome c oxidase in solution during the F-->O transition.
| Autoři: | Zaslavsky D; Department of Biochemistry, University of Illinois, 600 South Mathews Street, Urbana, IL 61801, USA., Sadoski RC, Rajagukguk S, Geren L, Millett F, Durham B, Gennis RB |
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| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2004 Jul 20; Vol. 101 (29), pp. 10544-7. Date of Electronic Publication: 2004 Jul 09. |
| Způsob vydávání: | Journal Article; Research Support, U.S. Gov't, P.H.S. |
| Jazyk: | English |
| Informace o časopise: | Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0027-8424 (Print) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Washington, DC : National Academy of Sciences |
| Výrazy ze slovníku MeSH: | Electron Transport* , Protons*, Electron Transport Complex IV/*metabolism, Animals ; Binding Sites ; Cattle ; Copper/chemistry ; Copper/metabolism ; Electron Transport Complex IV/chemistry ; Heme/chemistry ; Heme/metabolism ; Light ; Oxidation-Reduction |
| Abstrakt: | The mechanism by which electron transfer is coupled to proton pumping in cytochrome c oxidase is a major unsolved problem in molecular bioenergetics. In this work it is shown that, at least under some conditions, proton release from the enzyme occurs before proton uptake upon electron transfer to the heme/Cu active site of the enzyme. This sequence is similar to that of proton release and uptake observed for the light-activated proton pump bacteriorhodopsin. In the case of cytochrome c oxidase, this observation means that both the ejected proton and the proton required for the chemistry at the enzyme active site must come from an internal proton pool. |
| References: | FEBS Lett. 2001 Sep 7;505(1):63-7. (PMID: 11557043) Nature. 1992 Mar 26;356(6367):301-9. (PMID: 1312679) J Bioenerg Biomembr. 1998 Feb;30(1):7-14. (PMID: 9623800) FEBS Lett. 2003 Nov 27;555(1):106-10. (PMID: 14630328) Biochemistry. 2002 Sep 24;41(38):11315-24. (PMID: 12234172) Biochemistry. 1999 Nov 16;38(46):15129-40. (PMID: 10563795) Biochim Biophys Acta. 1998 Jul 20;1365(3):421-34. (PMID: 9711295) Proc Natl Acad Sci U S A. 2003 Jul 22;100(15):8715-20. (PMID: 12851460) FEBS Lett. 2003 Nov 27;555(1):8-12. (PMID: 14630311) FEBS Lett. 2003 Nov 27;555(1):29-34. (PMID: 14630314) Biochemistry. 2002 Jan 22;41(3):967-73. (PMID: 11790120) Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15543-7. (PMID: 14676323) Nature. 1995 Aug 24;376(6542):660-9. (PMID: 7651515) Biochemistry. 1988 Sep 20;27(19):7180-4. (PMID: 2849987) Biochemistry. 2001 Dec 18;40(50):15086-97. (PMID: 11735391) Chem Rev. 1996 Nov 7;96(7):2889-2908. (PMID: 11848844) Biochim Biophys Acta. 2003 Jun 5;1604(2):61-5. (PMID: 12765763) Proc Natl Acad Sci U S A. 1998 Nov 10;95(23):13606-11. (PMID: 9811847) Biochim Biophys Acta. 2000 Aug 15;1459(2-3):533-9. (PMID: 11004473) Curr Opin Struct Biol. 2000 Dec;10(6):672-9. (PMID: 11114504) Science. 2003 Aug 1;301(5633):610-5. (PMID: 12893935) FEBS Lett. 1993 Dec 28;336(3):389-93. (PMID: 8282099) Biochemistry. 1998 Oct 20;37(42):14910-6. (PMID: 9778367) FEBS Lett. 2004 May 21;566(1-3):126-30. (PMID: 15147881) Ann N Y Acad Sci. 1988;550:124-38. (PMID: 2854384) Biochemistry. 2004 Feb 3;43(4):1003-9. (PMID: 14744145) FEBS Lett. 2003 Nov 27;555(1):111-5. (PMID: 14630329) J Mol Biol. 2003 Apr 25;328(2):439-50. (PMID: 12691752) Biochemistry. 2003 Jul 29;42(29):8809-17. (PMID: 12873142) Proc Natl Acad Sci U S A. 1992 Jul 15;89(14):6497-501. (PMID: 1321442) J Biol Chem. 2001 Sep 7;276(36):33616-20. (PMID: 11443122) |
| Grant Information: | P20 RR015569 United States RR NCRR NIH HHS; HL16101 United States HL NHLBI NIH HHS; F32 GM020488 United States GM NIGMS NIH HHS; GM20488 United States GM NIGMS NIH HHS; R01 GM020488 United States GM NIGMS NIH HHS; R01 HL016101 United States HL NHLBI NIH HHS; R37 HL016101 United States HL NHLBI NIH HHS; 1P20 RR15569 United States RR NCRR NIH HHS |
| Substance Nomenclature: | 0 (Protons) 42VZT0U6YR (Heme) 789U1901C5 (Copper) EC 1.9.3.1 (Electron Transport Complex IV) |
| Entry Date(s): | Date Created: 20040713 Date Completed: 20040826 Latest Revision: 20240314 |
| Update Code: | 20240314 |
| PubMed Central ID: | PMC489974 |
| DOI: | 10.1073/pnas.0401521101 |
| PMID: | 15247424 |
| Autor: | Zaslavsky D; Department of Biochemistry, University of Illinois, 600 South Mathews Street, Urbana, IL 61801, USA., Sadoski RC, Rajagukguk S, Geren L, Millett F, Durham B, Gennis RB |
| Jazyk: | angličtina |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2004 Jul 20; Vol. 101 (29), pp. 10544-7. Date of Electronic Publication: 2004 Jul 09. |
| DOI: | 10.1073/pnas.0401521101 |
| Abstrakt: | The mechanism by which electron transfer is coupled to proton pumping in cytochrome c oxidase is a major unsolved problem in molecular bioenergetics. In this work it is shown that, at least under some conditions, proton release from the enzyme occurs before proton uptake upon electron transfer to the heme/Cu active site of the enzyme. This sequence is similar to that of proton release and uptake observed for the light-activated proton pump bacteriorhodopsin. In the case of cytochrome c oxidase, this observation means that both the ejected proton and the proton required for the chemistry at the enzyme active site must come from an internal proton pool. |
| Databáze: | MEDLINE |
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