Preparation and properties of three pure crystalline bacterial haem proteins

Horio, Takekazu; Kamen, Martin D.

doi:10.1016/0006-3002(61)90476-0

Cited by 166 publications

(53 citation statements)

References 15 publications

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“…The resulting extract was dialyzed against 10 mM Tris/HCl pH 8.0 and loaded onto a column (5 X 20 cm) of DEAE-Sephadex (Pharmacia) equilibrated with 10 mM Tris/HCl pH 8.0. The bright red fraction which did not bind to this anion exchanger was loaded onto an aluminum oxide column (3x6 cm; Merck), activated according to Horio and Kamen [18] and equilibrated with 10 mM Tris/HCl pH 8.0. The cytochrome fraction was eluted with 1 M potassium phosphate pH 7.0 and concentrated in an Amicon stirred cell equipped with a YM 5 membrane.…”

Section: Methodsmentioning

confidence: 99%

Cytochrome c₅₅₃ from Desulfovibrio vulgaris (Hildenborough)

Verhagen

Wolbert

Hagen

1994

European Journal of Biochemistry

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An electrochemical study of the periplasmic cytochrome c553 of Desulfovibrio vulgaris (Hildenborough) is presented. The dependence of the midpoint potential on temperature and pH was studied with cyclic voltammetry. The voltammograms obtained were reversible and revealed that this cytochrome showed fast electron transfer on a bare glassy carbon electrode. The midpoint potential at pH 7.0 and 25°C was found to be 62 mV versus the normal hydrogen electrode. It was observed that the temperature dependence was discontinuous with a transition temperature at 32°C. The standard reaction entropy at the growth temperature of the organism (37°C) was calculated to be AS"'= -234 J mol-' K-I. The pH dependence of the midpoint potential could be described with one pK of the oxidized form with a value of 10.6. The second-order rate constant for electron transfer between cytochrome css3 and the Fe-hydrogenase from D. vulgaris (H) was also determined with cyclic voltammetry. The equivalent rate constant for cytochrome c3 and hydrogenase was measured for comparison. The second-order rate constants are 2X 1O'M-I s-' for cytochrome c5s3 and 2X 10' M-' s-' for cytochrome c3. The kinetic parameters of the hydrogenase for both cytochromes were determined using the spectrophotometric hydrogen consumption assay. With cytochrome css3 this resulted in a K, of 46 pM and a maximum turnover number of 7

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Section: Methodsmentioning

confidence: 99%

Cytochrome c₅₅₃ from Desulfovibrio vulgaris (Hildenborough)

Verhagen

Wolbert

Hagen

1994

European Journal of Biochemistry

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“…Horio and Kamen [9] showed that the spectrum of ferricytochrome c does change in alkaline pH. We found that the 697 nm band disappears in a single step ionisation with an approx.…”

Section: Discussionmentioning

confidence: 63%

Conformation changes in cytochrome c₂ from Rhodospirillum rubrum

Pettigrew¹,

Schejter²

1974

FEBS Letters

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“…Cloning and site-directed mutagenesis of the Chromatium vinosum cytochrome c' have made it possible to establish the relationship between structure and physicochemical properties of the cytochrome c' (Even, Kassner, Dolata, Meyer & Cusanovich, 1996). Since the heme Fe atom of cytochromes c' is in the high-spin state (Taniguchi & Kamen, 1963), they have unique spectroscopic (Horio & Kamen, 1961;Imai, Imai, Sato & Horio, 1969) and ligand-binding properties (Cusanovich & Gibson, 1973) compared with class I cytochromes c.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray study of a new crystal form of cytochrome c' from Rhodobacter capsulatus

Higuchi¹,

Okama²,

Kanda³

et al. 1996

Acta Cryst D

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A new crystal form of diheme cytochrome c' from Rhodobacter capsulatus has been obtained and preliminary crystallographic experiments have been performed. The crystals belong to the space group P2~2~2 with unit-cell dimensions of a = 47.82, b = 72.59, c = 34.32 ~,. The assumption that an asymmetric unit of the crystal contains "one half of the homodimer molecule indicates that the monomers in the dimeric molecule may be related by a crystallographic twofold axis. Crystals diffract up to 1.7 A resolution using the X-ray beam from synchrotron radiation, and 11 127 unique structure factors were obtained with an Rmerg e of 7.1% from 52922 indexed reflections. Structure analysis by means of molecular-replacement methods is now underway.

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Preparation and properties of three pure crystalline bacterial haem proteins

Cited by 166 publications

References 15 publications

Cytochrome c₅₅₃ from Desulfovibrio vulgaris (Hildenborough)

Cytochrome c₅₅₃ from Desulfovibrio vulgaris (Hildenborough)

Conformation changes in cytochrome c₂ from Rhodospirillum rubrum

Crystallization and preliminary X-ray study of a new crystal form of cytochrome c' from Rhodobacter capsulatus

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Preparation and properties of three pure crystalline bacterial haem proteins

Cited by 166 publications

References 15 publications

Cytochrome c553 from Desulfovibrio vulgaris (Hildenborough)

Cytochrome c553 from Desulfovibrio vulgaris (Hildenborough)

Conformation changes in cytochrome c2 from Rhodospirillum rubrum

Crystallization and preliminary X-ray study of a new crystal form of cytochrome c' from Rhodobacter capsulatus

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Cytochrome c₅₅₃ from Desulfovibrio vulgaris (Hildenborough)

Cytochrome c₅₅₃ from Desulfovibrio vulgaris (Hildenborough)

Conformation changes in cytochrome c₂ from Rhodospirillum rubrum