Spectroscopic Investigation of Rubredoxin and Ferredoxin

Atherton, N. M.; Garbett, K.; Gillard, R. D.; Mason, R.; Mayhew, S. J.; Peel, J. L.; Stangroom, J. E.

doi:10.1038/212590a0

Cited by 52 publications

(16 citation statements)

References 5 publications

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“…This spectrum is similar to those of other rubredoxins (e.g. Atherton et al, 1966). There is a small difference between the spectra of the oxidized forms of Ch.…”

Section: Optical Spectra Of the Rubredoxinsupporting

confidence: 82%

Mössbauer effect in rubredoxin. Determination of the hyperfine field of the iron in a simple iron–sulphur protein

Rao

Evans

Cammack

et al. 1972

Biochemical Journal

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1. Rubredoxin isolated from the green photosynthetic bacterium Chloropseudomonas ethylica was similar in composition to those from anaerobic fermentative bacteria. Amino acid analysis indicated a minimum molecular weight of 6352 with one iron atom per molecule. 2. The circular-dichroism and electron-paramagnetic-resonance spectra of Ch. ethylica rubredoxin showed many similarities to those of Clostridium pasteurianum, but suggested that there may be subtle differences in the protein conformation about the iron atom. 3. Mössbauer-effect measurements on rubredoxin from Cl. pasteurianum and Ch. ethylica showed that in the oxidized state the iron (high-spin Fe(3+)) has a hyperfine field of 370+/-3kG, whereas in the reduced state (high-spin Fe(2+)) the hyperfine field tensor is anisotropic with a component perpendicular to the symmetry axis of the ion of about -200kG. For the reduced protein the sign of the electric-field gradient is negative, i.e. the ground state of the Fe(2+) is a [unk] orbital. There is a large non-cubic ligand-field splitting (Delta/k=900 degrees K), and a small spin-orbit splitting (D~+4.4cm(-1)) of the Fe(2+) levels. 4. The contributions of core polarization to the hyperfine field in the Fe(3+) and Fe(2+) ions are estimated to be -370 and -300kG respectively. 5. The significance of these results in interpretation of the Mössbauer spectra of other iron-sulphur proteins is discussed.

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“…This spectrum is similar to those of other rubredoxins (e.g. Atherton et al, 1966). There is a small difference between the spectra of the oxidized forms of Ch.…”

Section: Optical Spectra Of the Rubredoxinsupporting

confidence: 82%

Mössbauer effect in rubredoxin. Determination of the hyperfine field of the iron in a simple iron–sulphur protein

Rao

Evans

Cammack

et al. 1972

Biochemical Journal

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“…Abbreviation: MDH, methanol dehydrogenase. (Mathur et al, 1966;Gray, 1964), and this idea has been extended by Atherton et al (1966) to the mechanism of reduction of rubredoxin.…”

Section: Resultsmentioning

confidence: 99%

The interaction between methanol dehydrogenase and the autoreducible cytochromes c of the facultative methylotroph Pseudomonas AM1

O'Keeffe¹,

Anthony²

1980

Biochemical Journal

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Cytochromes cH and cL were autoreduced at high pH (pK greater than 10) and the autoreduced cytochromes reacted with CO. The autoreduction was first-order with respect to oxidized cytochrome c and was reversible by lowering the pH. Pure methanol dehydrogenase reduced cytochrome c (in the absence of methanol) by lowering the pK for autoreduction to less than 8.5. A mechanism is proposed for the autoreduction of cytochrome c and its involvement in the reaction with methanol dehydrogenase.

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“…562 CD spectra of rubredoxins display minima at 202 and 226 nm from β-sheet structures in the protein. 620−622 …”

Section: Fe–s Redox Centers In Electron Transfer Processesmentioning

confidence: 99%

Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers

et al. 2014

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Blue Type I Copper Centers vs Purple Cu A Centers 4439 5. Enzymes Employing a Combination of Different Types of Electron Transfer Centers 4439 5.1. Enzymes Using Both Heme and Cu as Electron Transfer Centers 4439 5.1.1. Cytochrome c and Cu A as Redox Partners to Cytochrome c Oxidases 4439 5.1.2. Cu A and Heme b as Redox Partners to Nitric Oxide Reductases 4440 5.1.3. Cytochrome c and Cu A as Redox Partners to Nitrous Oxide Reductases 4440 5.2. Enzymes Using Both Heme and Iron−Sulfur Clusters as Electron Transfer Centers 4440 5.2.1. As Redox Partners to the Cytochrome bc 1 Complex 4440 5.2.2. As Redox Partners to the Cytochrome b 6 f Complex 4442 5.2.3. As Redox Centers in Formate Dehydrogenases 4443 5.2.4. As Redox Centers in Nitrate Reductase 4443 6. Summary and Outlook 4443 Author Information 4445 Corresponding Author 4445 Author Contributions 4445 Notes 4445 Biographies 4445 Acknowledgments 4447 Abbreviations 4447 References 4447

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Spectroscopic Investigation of Rubredoxin and Ferredoxin

Cited by 52 publications

References 5 publications

Mössbauer effect in rubredoxin. Determination of the hyperfine field of the iron in a simple iron–sulphur protein

Mössbauer effect in rubredoxin. Determination of the hyperfine field of the iron in a simple iron–sulphur protein

The interaction between methanol dehydrogenase and the autoreducible cytochromes c of the facultative methylotroph Pseudomonas AM1

Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers

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