On the anomalous interactions of ligands with rhodospirillum haem protein

Taniguchí, Shinkichi; Kamen, Martin D.

doi:10.1016/0006-3002(63)91387-8

Cited by 68 publications

(33 citation statements)

References 14 publications

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“…A great many subsequent experiments also yield results similarly intermediate between those of the high-spin and low-spin classes. Though cytochrome c', like myoglobin, binds CO in the reduced form, it has a much lower affinity (Taniguchi & Kamen, 1963). In the ferric state, however, it shares with cytochrome c the resistance to coordination with ionic ligands which bind readily to the prototype high-spin proteins.…”

Section: Cytochromes C'mentioning

confidence: 99%

The spin 3/2 state and quantum spin mixtures in haem proteins

Maltempo

Moss

1976

Quart. Rev. Biophys.

188

118

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The magnetic state of iron in haem proteins has long been recognized as a convenient indicator of chemical coordination as well as more subtle biochemical properties. In the trivalent case in particular, there are three magnetically distinct configurations of the five 3d electrons, yielding spin states of S = 1/2, 3/2 and 5/2. The first and third are extremely familiar, and often lie close enough in energy so that a thermal mixture of low-spin S = 1/2 and high-spin S = 5/2 states exists in an ensemble of molecules. Selection rules for common perturbations (ΔS = ∘, ± 1 for the spin-orbit interaction and ΔS = ∘ for the electronic Zeeman interaction) ensure that quantum mixtures, in which the wave function is a true combination of S = 1/2 and S = 5/2 components, are not observed. The mid-spin, S = 3/2, state, and allowed 5/2–3/2 and 1/2–3/2 quantum mixtures including it, are much less well known. These have only rarely been invoked in recent years as an explanation for experimental haem protein magnetic data.

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Section: Cytochromes C'mentioning

confidence: 99%

The spin 3/2 state and quantum spin mixtures in haem proteins

Maltempo

Moss

1976

Quart. Rev. Biophys.

188

118

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“…The function of cytochrome c' in denitrifying bacteria can perhaps be seen in its ability to bind NO during the reduction of nitrite to nitrogen [42], In phototrophic bacteria cytochrome c' m ight be involved not only in nitrogen m etabolism but also in sulfur metabolism. In Chr.…”

Section: Discussionmentioning

confidence: 99%

Cytochromes and Anaerobic Sulfide Oxidation in the Purple Sulfur Bacterium Chromatium warmingii

Wermter

Fischer

1983

Zeitschrift Für Naturforschung C

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Chromatium warmingii, Cytochrome c', Cytochrom e c-552, A naerobic Sulfide O xidation, Phototrophic Bacteria Two soluble acidic c-type cytochromes -c' and c-552 -were isolated by ion exchange chromatography, gel filtration and amm onium sulfate fractionation. Cytochrom e c' is a high-spin cytochrome with maxima at 399 nm, 490 nm, and 634 nm in the oxidized form and at 550 nm, 425 nm and a characteristic shoulder at 434 nm in the reduced state. The best purity index obtained (^280/^399) was 0.35. Cytochrome c' is autoxidizable, has a m olecular weight of 12000 (estimated by sodium dodecylsulfate electrophoresis), a m idpoint redoxpotential o f + 10m V and an iso electric point at pH 4.0. The reduced cytochrome c' reacts with carbon monoxide. The reaction is reversible. Cytochrome c-552 shows maxima at 552 nm, 523 nm and 417 nm in the reduced form and at 408 nm in the oxidized state. The best purity index obtained (^280/^408) was 0.94. Cytochrome c-552 has a molecular weight of 30000 and an isoelectric point between pH 4.3 and 5.0.Chromatium warmingii also contains a m em brane-bound cytochrom e c-552. D uring anaerobic sulfide oxidation, elemental sulfur and sulfate were formed at the sam e time. W hen all sulfide was consumed by the cells, the remaining intracellular elemental sulfur was further oxidized to sulfate. IntroductionReduced sulfur compounds, like sulfide or thiosulfate, are used as electron donors for anoxygenic photosynthesis by phototrophic sulfur bacteria [1,2]. Electron transfer proteins, like cytochromes or high potential iron sulfur proteins, are generally involved in sulfur metabolism in purple and green sulfur bacteria [2,3], The m olecular properties of cytochromes, their distribution and their function in sulfide and thiosulfate oxidation in green sulfur bacteria (Chlorobiaceae) have been intensively studied [4][5][6][7][8][9][10][11][12][13], In these organisms, flavocytochromes act as sulfide: cytochrome c reductases [7,[9][10][11], Cytochrome c-551, only present in the thiosulfate utilizing Chlorobium limicola f thiosulfcitophilum [6,9] and Chlorobium vibrioforme f. thiosulfatopliilum [11] is the only endogenous electron acceptor in thiosulfate oxidation. A small Abbreviations: Chr. Chromatium ; APS, adenylylsulfate; SDS, sodium dodecylsulfate.Reprint requests to Dr. U. Fischer.0341-0382/83/1100-0960 $ 0 1 .3 0 /0 cytochrome c-555, com parable to plant /-type cyto chromes, was found in all green sulfur bacteria and functions as an electron mediator. It accepts the electrons from both cytochromes mentioned above and carries them to bacteriochlorophyll [8,9,13].Cytochromes of the purple sulfur bacteria (Chromatiaceae) have been isolated so far only from small-cell species, like Chromatium vinosum [14][15][16][17] U. Wermter and U. Fischer • Cytochromes and Anaerobic Su lfid e O xidation in Chromatium warmingii 961cytochrome content. The aim of this study was, to isolate and to characterize the cytochromes of Cliromatium warmingii and to com pare the results with those of the small-cell Ch...

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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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On the anomalous interactions of ligands with rhodospirillum haem protein

Cited by 68 publications

References 14 publications

The spin 3/2 state and quantum spin mixtures in haem proteins

The spin 3/2 state and quantum spin mixtures in haem proteins

Cytochromes and Anaerobic Sulfide Oxidation in the Purple Sulfur Bacterium Chromatium warmingii

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

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