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Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c.

ABSTRACT: The cytochrome bc1 complex (ubiquinone:cytochrome c oxidoreductase) is the central integral membrane protein in the mitochondrial respiratory chain as well as the electron-transfer chains of many respiratory and photosynthetic prokaryotes. Based on X-ray crystallographic studies of cytochrome bc1, a mechanism has been proposed in which the extrinsic domain of the iron-sulfur protein first binds to cytochrome b where it accepts an electron from ubiquinol in the Qo site, and then rotates by 57° to a position close to cytochrome c1 where it transfers an electron to cytochrome c1. This review describes the development of a ruthenium photooxidation technique to measure key electron transfer steps in cytochrome bc1, including rapid electron transfer from the iron-sulfur protein to cytochrome c1. It was discovered that this reaction is rate-limited by the rotational dynamics of the iron-sulfur protein rather than true electron transfer. A conformational linkage between the occupant of the Qo ubiquinol binding site and the rotational dynamics of the iron-sulfur protein was discovered which could play a role in the bifurcated oxidation of ubiquinol. A ruthenium photoexcitation method is also described for the measurement of electron transfer from cytochrome c1 to cytochrome c. This article is part of a Special Issue entitled: Respiratory Complex III and related bc complexes.

SUBMITTER: Millett F

PROVIDER: S-EPMC3535674 | biostudies-literature | 2013 Nov-Dec

REPOSITORIES: biostudies-literature

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Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c.

Millett Francis F Havens Jeffrey J Rajagukguk Sany S Durham Bill B

Biochimica et biophysica acta 20120915 11-12

The cytochrome bc1 complex (ubiquinone:cytochrome c oxidoreductase) is the central integral membrane protein in the mitochondrial respiratory chain as well as the electron-transfer chains of many respiratory and photosynthetic prokaryotes. Based on X-ray crystallographic studies of cytochrome bc1, a mechanism has been proposed in which the extrinsic domain of the iron-sulfur protein first binds to cytochrome b where it accepts an electron from ubiquinol in the Qo site, and then rotates by 57° to ...[more]

PMID: 22985600

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Project description:Ruthenium(II) complexes having pterins of redox-active heteroaromatic coenzymes as ligands were demonstrated to perform multistep proton transfer (PT), electron transfer (ET), and proton-coupled electron transfer (PCET) processes. Thermodynamic parameters including pK(a) and bond dissociation energy (BDE) of multistep PCET processes in acetonitrile (MeCN) were determined for ruthenium-pterin complexes, [Ru(II)(Hdmp)(TPA)](ClO(4))(2) (1), [Ru(II)(Hdmdmp)(TPA)](ClO(4))(2) (2), [Ru(II)(dmp(-))(TPA)]ClO(4) (3), and [Ru(II)(dmdmp(-))(TPA)]ClO(4) (4) (Hdmp = 6,7-dimethylpterin, Hdmdmp = N,N-dimethyl-6,7-dimethylpterin, TPA = tris(2-pyridylmethyl)amine), all of which had been isolated and characterized before. The BDE difference between 1 and one-electron oxidized species, [Ru(III)(dmp(-))(TPA)](2+), was determined to be 89 kcal mol(-1), which was large enough to achieve hydrogen atom transfer (HAT) from phenol derivatives. In the HAT reactions from phenol derivatives to [Ru(III)(dmp(-))(TPA)](2+), the second-order rate constants (k) were determined to exhibit a linear relationship with BDE values of phenol derivatives with a slope (-0.4), suggesting that this HAT is simultaneous proton and electron transfer. As for HAT reaction from 2,4,6-tri-tert-buthylphenol (TBP; BDE = 79.15 kcal mol(-1)) to [Ru(III)(dmp(-))(TPA)](2+), the activation parameters were determined to be DeltaH(double dagger) = 1.6 +/- 0.2 kcal mol(-1) and DeltaS(double dagger) = -36 +/- 2 cal K(-1) mol(-1). This small activation enthalpy suggests a hydrogen-bonded adduct formation prior to HAT. Actually, in the reaction of 4-nitrophenol with [Ru(III)(dmp(-))(TPA)](2+), the second-order rate constants exhibited saturation behavior at higher concentrations of the substrate, and low-temperature ESI-MS allowed us to detect the hydrogen-bonding adduct. This also lends credence to an associative mechanism of the HAT involving intermolecular hydrogen bonding between the deprotonated dmp ligand and the phenolic O-H to facilitate the reaction. In particular, a two-point hydrogen bonding between the complex and the substrate involving the 2-amino group of the deprotonated pterin ligand effectively facilitates the HAT reaction from the substrate to the Ru(III)-pterin complex.

Dataset Information

Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c.

Publications

Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c.

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