Homotropic and heterotropic interactions in cytochromes <i>c</i><sub>3</sub> from sulphate reducing bacteria

Turner, David L.; Catarino, Teresa

doi:10.1016/j.febslet.2011.07.007

Cited by 4 publications

(7 citation statements)

References 38 publications

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“…Cytochrome c 3 has been extensively studied in X-band EPR (see below) and has been scrutinized as a paradigm for redox interaction in biological electron transfer. 19 …”

Section: Resultsmentioning

confidence: 99%

“…Cytochrome c 3 is readily obtained in large quantities from sulfate-reducing bacteria and has a longstanding status as paradigmatic redox interaction protein: its single-electron transferring hemes cooperate to form a de facto electron-pair donor/acceptor system for enzymes, such as hydrogenase, that catalyze redox reactions involving two reducing equivalents. 19 …”

Section: Resultsmentioning

confidence: 99%

“…vulgaris substrain Hildenborough) cytochrome c 3 , which is also a small (14 kDa), sturdy protein without tendency to polymerize but containing four hemes per protein molecule. Cytochrome c 3 has been extensively studied in X-band EPR (see below) and has been scrutinized as a paradigm for redox interaction in biological electron transfer …”

Section: Resultsmentioning

confidence: 99%

“…In addition to this “biological wire” function, they may also exhibit more complex mechanisms of action by means of redox interaction, that is, (anti-) cooperativity in reduction potentials. Cytochrome c 3 is readily obtained in large quantities from sulfate-reducing bacteria and has a longstanding status as paradigmatic redox interaction protein: its single-electron transferring hemes cooperate to form a de facto electron-pair donor/acceptor system for enzymes, such as hydrogenase, that catalyze redox reactions involving two reducing equivalents …”

Section: Resultsmentioning

confidence: 99%

“…Cytochrome c 3 has been extensively studied in X-band EPR (see below) and has been scrutinized as a paradigm for redox interaction in biological electron transfer. 19 Using four different spectrometers, we have previously shown that the sharpest feature (the g z peak) in the spectrum of cytochrome c is virtually invariant on a reciprocal g-value scale from 35 to 1 GHz. 6 This finding has now been confirmed for the complete spectrum as I find, in an overlay of 9.4 and 1.1 GHz data, only a marginal extra broadening in the low-frequency spectrum (Figure S5).…”

Section: The Journal Of Physical Chemistrymentioning

confidence: 99%

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Very Low-Frequency Broadband Electron Paramagnetic Resonance Spectroscopy of Metalloproteins

Hagen

2021

J. Phys. Chem. A

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A previously developed spectrometer for broadband electron paramagnetic resonance (EPR) spectroscopy of dilute randomly oriented systems has been considerably modified to extend the frequency reach down to the hundred MHz range and to boost concentration sensitivity by 1 to 2 orders of magnitude. The instrument is now suitable for the study of biological systems in particular metalloproteins. As a proof of concept, examples from the class of low-spin ferric hemoproteins are studied in terms of frequency-dependent changes in their EPR spectra. Mono-heme cytochrome c EPR is determined by g-strain over a wide frequency range, whereas a combination of unresolved ligand hyperfine interaction and concentration-dependent intermolecular dipolar interaction becomes dominant at very low frequencies. In the four heme containing cytochrome c 3 , g-strain combines with intramolecular dipolar interaction over the full-studied frequency range of 0.23–12.0 GHz. It is concluded that the point-dipole approach is inappropriate to describe magnetic interactions between low-spin ferric heme systems and that a body of literature on redox interactions in multi-heme proteins will be affected by this conclusion.

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“…Cytochrome c 3 has been extensively studied in X-band EPR (see below) and has been scrutinized as a paradigm for redox interaction in biological electron transfer. 19 …”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: The Journal Of Physical Chemistrymentioning

confidence: 99%

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Very Low-Frequency Broadband Electron Paramagnetic Resonance Spectroscopy of Metalloproteins

Hagen

2021

J. Phys. Chem. A

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Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

et al. 2016

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In the present work, Ion Jelly films based on 1‐ethyl‐3‐methylimidazolium ethylsulfate, with incorporated redox proteins and enzymes were deposited on carbon screen‐printed electrodes (SPEs), and their electrochemical characterization was attained. Ion Jelly synthesis was carried out simultaneously with protein incorporation in its structure, followed by a maturation step under controlled atmosphere (4 days at 4 °C and water activity (aw) of 0.76). The electrochemical response of the material was characterized, and a sandwich‐type fuel cell configuration was subsequently built, consisting of two SPEs containing two independent Ion Jelly discs in the middle; one disc incorporated Desulfovibrio gigas cytochrome c3 and [NiFe]‐hydrogenase, while the other disc contained aldehyde oxidoreductase, constituting the biocathode and bioanode of the cell, respectively. Cell voltage increased with time in the presence of benzaldehyde, in agreement with a successful electronic pathway across the cell and the concomitant aldehyde oxidoreductase enzymatic activity. In the cathodic side assays, hydrogenase showed catalytic activity towards H+ reduction to H2.

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Electron transfer between multihaem cytochromes c3 from Desulfovibrio africanus

Quintas

Oliveira

Catarino

et al. 2013

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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The tetrahaem type I cytochromes c3 from Desulfovibrionaceae shuttle electrons from a periplasmic hydrogenase to transmembrane electron transfer complexes. In D. africanus, it is believed that the electrons are received by another tetrahaem cytochrome c3, denoted type II, which is associated with the membrane complex. Thermodynamic measurements show that the type I cytochrome c3 has the potential to transfer two electrons at a time. This study uses two-dimensional NMR to investigate the exchange of electrons between type I and type II cytochromes c3 at equilibrium in intermediate stages of oxidation. The results indicate that the two proteins are physiological partners but that only single-electron transfers occur in solution.

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Homotropic and heterotropic interactions in cytochromes c₃ from sulphate reducing bacteria

Cited by 4 publications

References 38 publications

Very Low-Frequency Broadband Electron Paramagnetic Resonance Spectroscopy of Metalloproteins

Very Low-Frequency Broadband Electron Paramagnetic Resonance Spectroscopy of Metalloproteins

Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

Electron transfer between multihaem cytochromes c3 from Desulfovibrio africanus

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Homotropic and heterotropic interactions in cytochromes c3 from sulphate reducing bacteria

Cited by 4 publications

References 38 publications

Very Low-Frequency Broadband Electron Paramagnetic Resonance Spectroscopy of Metalloproteins

Very Low-Frequency Broadband Electron Paramagnetic Resonance Spectroscopy of Metalloproteins

Sandwich-Type Enzymatic Fuel Cell Based on a New Electro-Conductive Material - Ion Jelly

Electron transfer between multihaem cytochromes c3 from Desulfovibrio africanus

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Homotropic and heterotropic interactions in cytochromes c₃ from sulphate reducing bacteria