Characterization of the pH-Dependent Resonance Raman Transitions of Archaeal and Bacterial Rieske [2Fe-2S] Proteins

Toshio Iwasaki; Asako Kounosu; Derrick R.J. Kolling; Antony R. Crofts; Sergei A. Dikanov; Akihisa Jin; Takeo Imai; Akio Urushiyama

doi:10.1021/ja031976p

Characterization of the pH-Dependent Resonance Raman Transitions of Archaeal and Bacterial Rieske [2Fe-2S] Proteins

Toshio Iwasaki, Asako Kounosu, Derrick R.J. Kolling, Antony R. Crofts, Sergei A. Dikanov, Akihisa Jin, Takeo Imai, Akio Urushiyama

Veterinary Clinical Medicine

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Abstract

The pH-dependent resonance Raman (RR) spectral changes of the cytochrome bc₁-associated, high-potential Rieske proteins have frequently been invoked to explain the redox-linked ionization behavior. We report herein RR spectral data of archaeal and bacterial Rieske proteins that directly demonstrate the pH-dependent changes near and above pK_a,ox2, but not around pK_a,ox1, of the visible circular dichroism (CD) transitions. The RR spectral changes are attributed to modification of the immediate [2Fe-2S] cluster environment due to deprotonation of some exchangeable amide groups in the polypeptide backbone, rather than previously assumed simple changes of the Fe-N_imid stretching vibrations.

Original language	English (US)
Pages (from-to)	4788-4789
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	126
Issue number	15
DOIs	https://doi.org/10.1021/ja031976p
State	Published - Apr 21 2004

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja031976p

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abstract = "The pH-dependent resonance Raman (RR) spectral changes of the cytochrome bc1-associated, high-potential Rieske proteins have frequently been invoked to explain the redox-linked ionization behavior. We report herein RR spectral data of archaeal and bacterial Rieske proteins that directly demonstrate the pH-dependent changes near and above pKa,ox2, but not around pKa,ox1, of the visible circular dichroism (CD) transitions. The RR spectral changes are attributed to modification of the immediate [2Fe-2S] cluster environment due to deprotonation of some exchangeable amide groups in the polypeptide backbone, rather than previously assumed simple changes of the Fe-Nimid stretching vibrations.",

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AU - Iwasaki, Toshio

AU - Kounosu, Asako

AU - Kolling, Derrick R.J.

AU - Crofts, Antony R.

AU - Dikanov, Sergei A.

AU - Jin, Akihisa

AU - Imai, Takeo

AU - Urushiyama, Akio

PY - 2004/4/21

Y1 - 2004/4/21

N2 - The pH-dependent resonance Raman (RR) spectral changes of the cytochrome bc1-associated, high-potential Rieske proteins have frequently been invoked to explain the redox-linked ionization behavior. We report herein RR spectral data of archaeal and bacterial Rieske proteins that directly demonstrate the pH-dependent changes near and above pKa,ox2, but not around pKa,ox1, of the visible circular dichroism (CD) transitions. The RR spectral changes are attributed to modification of the immediate [2Fe-2S] cluster environment due to deprotonation of some exchangeable amide groups in the polypeptide backbone, rather than previously assumed simple changes of the Fe-Nimid stretching vibrations.

AB - The pH-dependent resonance Raman (RR) spectral changes of the cytochrome bc1-associated, high-potential Rieske proteins have frequently been invoked to explain the redox-linked ionization behavior. We report herein RR spectral data of archaeal and bacterial Rieske proteins that directly demonstrate the pH-dependent changes near and above pKa,ox2, but not around pKa,ox1, of the visible circular dichroism (CD) transitions. The RR spectral changes are attributed to modification of the immediate [2Fe-2S] cluster environment due to deprotonation of some exchangeable amide groups in the polypeptide backbone, rather than previously assumed simple changes of the Fe-Nimid stretching vibrations.

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Characterization of the pH-Dependent Resonance Raman Transitions of Archaeal and Bacterial Rieske [2Fe-2S] Proteins

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