Review
doi: 10.1007/BF00762859.
Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation
Affiliations
- PMID: 8389750
- DOI: 10.1007/BF00762859
Item in Clipboard
Review
Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation
J Bioenerg Biomembr.
1993 Apr.
Abstract
Results are presented which, taken with evidence developed by others, suggest a general mechanism for the entry and binding of exogenous ligands (including O2) at the "binuclear site" (CuBFea3) of the heme-copper oxidases. The mechanism includes a "ligand shuttle" wherein the obligatory way station for incoming ligands is CuB and the binding of exogenous ligands at this site triggers the exchange and displacement of endogenous ligands at Fea3. It is suggested that these ligand shuttle reactions might be functionally important in providing a coupling mechanism for electron transfer and proton translocation. Scenarios as to how this might happen are delineated.
Similar articles
-
Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers.J Inorg Biochem. 2000 Nov;82(1-4):19-25. doi: 10.1016/s0162-0134(00)00140-9. J Inorg Biochem. 2000. PMID: 11132627 Review.
-
The gateway to the active site of heme-copper oxidases.Biochemistry. 1993 Nov 16;32(45):11953-6. doi: 10.1021/bi00096a002. Biochemistry. 1993. PMID: 8218269
-
Fourier-transform infrared study of cyanide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: implication of the redox-linked conformational change at the binuclear site.Biochemistry. 1993 Jan 12;32(1):164-73. doi: 10.1021/bi00052a022. Biochemistry. 1993. PMID: 8380331
-
Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: a general mechanism for the interaction of copper proteins with nitric oxide?FEBS Lett. 1997 Sep 8;414(2):281-4. doi: 10.1016/s0014-5793(97)01009-0. FEBS Lett. 1997. PMID: 9315702
-
Cooperative coupling and role of heme a in the proton pump of heme-copper oxidases.Biochimie. 1998 Oct;80(10):821-36. doi: 10.1016/s0300-9084(00)88877-x. Biochimie. 1998. PMID: 9893941 Review.
Cited by
-
Isolation of yeast complex IV in native lipid nanodiscs.Biochim Biophys Acta. 2016 Dec;1858(12):2984-2992. doi: 10.1016/j.bbamem.2016.09.004. Epub 2016 Sep 13. Biochim Biophys Acta. 2016. PMID: 27620332 Free PMC article.
-
Probing protonation/deprotonation of tyrosine residues in cytochrome ba3 oxidase from Thermus thermophilus by time-resolved step-scan Fourier transform infrared spectroscopy.J Biol Chem. 2011 Sep 2;286(35):30600-30605. doi: 10.1074/jbc.M111.252213. Epub 2011 Jul 12. J Biol Chem. 2011. PMID: 21757723 Free PMC article.
-
The rate-limiting step in O(2) reduction by cytochrome ba(3) from Thermus thermophilus.Biochim Biophys Acta. 2012 Apr;1817(4):666-71. doi: 10.1016/j.bbabio.2011.11.010. Epub 2011 Nov 27. Biochim Biophys Acta. 2012. PMID: 22138627 Free PMC article.
-
Mutation of a single residue in the ba3 oxidase specifically impairs protonation of the pump site.Proc Natl Acad Sci U S A. 2015 Mar 17;112(11):3397-402. doi: 10.1073/pnas.1422434112. Epub 2015 Mar 2. Proc Natl Acad Sci U S A. 2015. PMID: 25733886 Free PMC article.
-
The heme-copper oxidases of Thermus thermophilus catalyze the reduction of nitric oxide: evolutionary implications.Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14718-23. doi: 10.1073/pnas.96.26.14718. Proc Natl Acad Sci U S A. 1999. PMID: 10611279 Free PMC article.