Literature DB >> 1330560

A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase.

W E Antholine1, D H Kastrau, G C Steffens, G Buse, W G Zumft, P M Kroneck.   

Abstract

The multicopper proteins, nitrous-oxide reductase (N2OR) and cytochrome c oxidase (COX), were investigated by EPR spectroscopy at microwave frequencies 2.4-35 GHz. Our results support a Cu-Cu interaction in COX and N2OR. At least 10 lines in the 2.7-GHz, 12 lines in the 4.6-GHz and 14 lines in the 9.2 GHz spectra were resolved for N2OR. Eight copper lines at 2.7 GHz, about nine lines at 4.6 GHz and about six lines at 9.2 GHz were resolved for COX. Simulations of the EPR spectra were consistent with most of the resonances of the multiline spectra, including regions in the center of the spectra where overlap of the three seven-line patterns is proposed. These simulations indicated that Cu-Cu interaction, in a mixed-valence [Cu(1.5) ... Cu(1.5)], S = 1/2 site is consistent with, if not proof of, the unusual spectral features observed for N2OR and COX.

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Year:  1992        PMID: 1330560     DOI: 10.1111/j.1432-1033.1992.tb17360.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  23 in total

1.  The second derivative electronic absorption spectrum of cytochrome c oxidase in the Soret region.

Authors:  M P Horvath; R A Copeland; M W Makinen
Journal:  Biophys J       Date:  1999-09       Impact factor: 4.033

2.  A new CuZ active form in the catalytic reduction of N(2)O by nitrous oxide reductase from Pseudomonas nautica.

Authors:  Simone Dell'Acqua; Sofia R Pauleta; Patrícia M Paes de Sousa; Enrico Monzani; Luigi Casella; José J G Moura; Isabel Moura
Journal:  J Biol Inorg Chem       Date:  2010-04-27       Impact factor: 3.358

3.  EPR Methods for Biological Cu(II): L-Band CW and NARS.

Authors:  Brian Bennett; Jason M Kowalski
Journal:  Methods Enzymol       Date:  2015-07-23       Impact factor: 1.600

Review 4.  Using synthetic chemistry to understand copper protein active sites: a personal perspective.

Authors:  William B Tolman
Journal:  J Biol Inorg Chem       Date:  2006-01-27       Impact factor: 3.358

Review 5.  The tetranuclear copper active site of nitrous oxide reductase: the CuZ center.

Authors:  Simone Dell'Acqua; Sofia R Pauleta; Isabel Moura; José J G Moura
Journal:  J Biol Inorg Chem       Date:  2011-01-15       Impact factor: 3.358

6.  Electron paramagnetic resonance studies of the soluble CuA protein from the cytochrome ba3 of Thermus thermophilus.

Authors:  M Karpefors; C E Slutter; J A Fee; R Aasa; B Källebring; S Larsson; T Vänngård
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

Review 7.  Walking the seven lines: binuclear copper A in cytochrome c oxidase and nitrous oxide reductase.

Authors:  Peter M H Kroneck
Journal:  J Biol Inorg Chem       Date:  2017-12-07       Impact factor: 3.358

8.  Electronic structure of the ground and excited states of the Cu(A) site by NMR spectroscopy.

Authors:  Luciano A Abriata; Gabriela N Ledesma; Roberta Pierattelli; Alejandro J Vila
Journal:  J Am Chem Soc       Date:  2009-02-11       Impact factor: 15.419

Review 9.  Crystal structure of bovine heart cytochrome c oxidase at 2.8 A resolution.

Authors:  S Yoshikawa; K Shinzawa-Itoh; T Tsukihara
Journal:  J Bioenerg Biomembr       Date:  1998-02       Impact factor: 2.945

10.  CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase.

Authors:  J A Farrar; W G Zumft; A J Thomson
Journal:  Proc Natl Acad Sci U S A       Date:  1998-08-18       Impact factor: 11.205

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