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Literature DB >> 11942802

Decay of the transient Cu(B)-CO complex is accompanied by formation of the heme Fe-CO complex of cytochrome cbb(3)-CO at ambient temperature: evidence from time-resolved Fourier transform infrared spectroscopy.

Stavros Stavrakis¹, Konstantinos Koutsoupakis, Eftychia Pinakoulaki, Andrea Urbani, Matti Saraste, Constantinos Varotsis.

Abstract

Time-resolved step-scan Fourier infrared spectroscopy has been used to study the CO-bound cbb(3)-type cytochrome c oxidase from Pseudomonas stutzeri at room temperature. We observe a single band in the FTIR spectrum at 1956 cm(-1) (beta-form). The time-resolved data indicate that upon photolysis, CO is transferred from heme b(3) (nu(CO) = 1956 cm(-1)) to CuB (nu(CO) = 2064 cm(-1)). The decay of the 2065 cm(-1) peak (t(1/2) = 120 +/- 16 ms) and the development of the 1956 cm(-1) peak (t(1/2) = 144 +/- 8 ms ) suggest that formation of the Fe-CO complex is concurrent with the decay of the CuB-CO complex. The intensity ratio of the Fe-CO/CuB-CO (2.15) remains constant for all data points, and thus we conclude that no fraction of CO escapes the binuclear center at 293 K.

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Year: 2002 PMID： 11942802 DOI： 10.1021/ja0169825

Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419

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Cited

10 in total

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2. Phase-sensitive detection in modulation excitation spectroscopy applied to potential induced electron transfer in cytochrome c oxidase.

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Authors: Young O Ahn; Paween Mahinthichaichan; Hyun Ju Lee; Hanlin Ouyang; Daniel Kaluka; Syun-Ru Yeh; Davinia Arjona; Denis L Rousseau; Emad Tajkhorshid; Pia Adelroth; Robert B Gennis
Journal: Proc Natl Acad Sci U S A Date: 2014-10-06 Impact factor: 11.205

4. Time-resolved surface-enhanced IR-absorption spectroscopy of direct electron transfer to cytochrome c oxidase from R. sphaeroides.

Authors: Andreas Schwaighofer; Christoph Steininger; David M Hildenbrandt; Johannes Srajer; Christoph Nowak; Wolfgang Knoll; Renate L C Naumann
Journal: Biophys J Date: 2013-12-17 Impact factor: 4.033

5. Structural changes that occur upon photolysis of the Fe(II)(a3)-CO complex in the cytochrome ba(3)-oxidase of Thermus thermophilus: a combined X-ray crystallographic and infrared spectral study demonstrates CO binding to Cu(B).

Authors: Bin Liu; Yang Zhang; J Timothy Sage; S Michael Soltis; Tzanko Doukov; Ying Chen; C David Stout; James A Fee
Journal: Biochim Biophys Acta Date: 2011-12-27

6. The diheme cytochrome c(4) from Vibrio cholerae is a natural electron donor to the respiratory cbb(3) oxygen reductase.

Authors: Hsin-Yang Chang; Young Ahn; Laura A Pace; Myat T Lin; Yun-Hui Lin; Robert B Gennis
Journal: Biochemistry Date: 2010-09-07 Impact factor: 3.162

Decay of the transient Cu(B)-CO complex is accompanied by formation of the heme Fe-CO complex of cytochrome cbb(3)-CO at ambient temperature: evidence from time-resolved Fourier transform infrared spectroscopy.

1. Probing protonation/deprotonation of tyrosine residues in cytochrome ba3 oxidase from Thermus thermophilus by time-resolved step-scan Fourier transform infrared spectroscopy.

2. Phase-sensitive detection in modulation excitation spectroscopy applied to potential induced electron transfer in cytochrome c oxidase.

3. Conformational coupling between the active site and residues within the K(C)-channel of the Vibrio cholerae cbb3-type (C-family) oxygen reductase.

4. Time-resolved surface-enhanced IR-absorption spectroscopy of direct electron transfer to cytochrome c oxidase from R. sphaeroides.

5. Structural changes that occur upon photolysis of the Fe(II)(a3)-CO complex in the cytochrome ba(3)-oxidase of Thermus thermophilus: a combined X-ray crystallographic and infrared spectral study demonstrates CO binding to Cu(B).

6. The diheme cytochrome c(4) from Vibrio cholerae is a natural electron donor to the respiratory cbb(3) oxygen reductase.

7. Kinetics and thermodynamics of formation and electron-transfer reactions of Cu-O₂ and Cu₂-O₂ complexes.

Review 8. Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.

9. Probing the Q-proton pathway of ba3-cytochrome c oxidase by time-resolved Fourier transform infrared spectroscopy.

10. Active site of cytochrome cbb3.