Purification of membrane‐bound cytochromes and a photoactive P840 protein complex of the green sulfur bacterium <i>Chlorobium limicola</i> f. <i>thiosulfatophilum</i>

Hurt, Eduard C.; Hauska, Günter

doi:10.1016/0014-5793(84)80225-2

Cited by 94 publications

(75 citation statements)

References 32 publications

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“…33 and Fig. 1B), or the b-type cytochrome from Chlorobium limicola, which shares intermediate properties between cytochrome b and cytochrome b 6 (57). The unusual stability of b heme binding to cytochrome b 6 strongly suggests some linkage that cannot be formed within cytochrome b from bc complexes.…”

Section: Discussionmentioning

confidence: 99%

Molecular Genetic Identification of a Pathway for Heme Binding to Cytochrome b 6

Kuras¹,

Vitry²,

Choquet³

et al. 1997

Journal of Biological Chemistry

100

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Heme binding to cytochrome b 6 is resistant, in part, to denaturing conditions that typically destroy the noncovalent interactions between the b hemes and their apoproteins, suggesting that one of two b hemes of holocytochrome b 6 is tightly bound to the polypeptide. We exploited this property to define a pathway for the conversion of apo-to holocytochrome b 6 , and to identify mutants that are blocked at one step of this pathway.

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Section: Discussionmentioning

confidence: 99%

Molecular Genetic Identification of a Pathway for Heme Binding to Cytochrome b 6

Kuras¹,

Vitry²,

Choquet³

et al. 1997

Journal of Biological Chemistry

100

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“…Its structure has not been resolved yet, although crystallization has been achieved (7,8). Interestingly, however, a similarity to the reaction center of green sulfur bacteria has been recognized (9)(10)(11)(12)(13)(14)(15). All the redox components known for PS1 (7,8), the "special pair" of chlorophylls as electron donor, A. and A1 as early electron acceptors, and the subsequent FeS centers X, A, and B, have also been detected in the green sulfur bacterium Chlorobium limicola (11,13), and they seem to exist as well in the distantly related Heliobacteria (14,16).…”

mentioning

confidence: 99%

“…All the redox components known for PS1 (7,8), the "special pair" of chlorophylls as electron donor, A. and A1 as early electron acceptors, and the subsequent FeS centers X, A, and B, have also been detected in the green sulfur bacterium Chlorobium limicola (11,13), and they seem to exist as well in the distantly related Heliobacteria (14,16). Moreover, the isolated reaction center from Chlorobium contains large subunits (10), very similar to PS1 preparations (17). The primary donor and the acceptors AO, A1, and X are thought to be located on these large subunits of PS1, while the two 4Fe4S centers A and B are contained in an extra subunit (7,8).…”

mentioning

confidence: 99%

Photosynthetic reaction center genes in green sulfur bacteria and in photosystem 1 are related.

Büttner

Xie

Nelson

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

201

113

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Oxygenic photosynthesis of chloroplasts and cyanobacteria involves two photosystems, which originate from different prokaryotic ancestors. The reaction center of photosystem 2 (PS2) is related to the well-characterized reaction center of purple bacteria, while the reaction center of photosystem 1 (PS1) is related to the green sulfur bacteria, as is convincingly documented here. An operon encoding the P840 reaction center of Chlorobium limicola f.sp. thiosulfatophilum has been cloned and sequenced. It contains two structural genes, coding for proteins of 730 and 232 amino acids. The first protein resembles the large subunits of the PS1 reaction center. Putative binding elements for the primary donor, P840 in Chlorobium and P700 in PS1, and for the acceptors A

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“…Whereas in membranes the peak of the rapidly photooxidised heme was consistently found at 553 nm (Fowler et al, 1971 ;Franken and Amesz, 1997;Okumura et al, 1994;Olson et al, 1976;Prince and Olson, 1976;Swarthoff et al, 1981), the cytochrome copurifying with the RC was mostly seen to have a-peaks in the region of 550.5-552 nm (Hager-Braun et al, 1995;Hurt and Hauska, 1984;Kusumoto et al, 1994;Oh-Oka et al, 1993;Okkels et al, 1992). Our results obtained on whole cells fully corroborate the data gathered on membranes.…”

Section: Discussionmentioning

confidence: 99%

Electron Transfer Towards the RCI‐Type Photosystem in the Green Sulphur Bacterium Chlorobium limicola Forma Thiosulphatophilum Studied by Time‐Resolved Optical Spectroscopy In Vivo

Albouy¹,

Joliot²,

Robert³

et al. 1997

European Journal of Biochemistry

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Flash-induced spectral changes in the wavelength region of the a-peaks of heme proteins and in the time domain from microseconds to seconds have been recorded on whole cells of the green sulphur bacterium Chlorobium lirnicola forma thiosu2fatophilurn.Extensive flash-excitation by trains of flashes resulted in oxidation of 7-8 c-type heme molecules/ photosynthetic reaction centre. The complement of heme species was found to be spectrally heterogeneous allowing the study of electron transfer events induced by an isolated single-turnover flash. Under singleflash conditions, a c551 heme was seen to become oxidised with z = 30 ps, concommitant with the reduction of the primary donor of the reaction centre. Subsequently, the a-peak of the photooxidised heme broadened and shifted towards longer wavelengths (z = 70 p) indicating equilibration of the positive charge over two differing heme species. In the time domain t > l ms, rereduction of c-type hemes was seen to be paralleled by a blue shift and further broadening of the a-peak. Concommitantly, b-type hemes were observed to first become reduced (within a few milliseconds), then over-oxidised (t>200 ms) and eventually rereduced to their redox state prior to the flash.The results obtained are discussed with respect to the question of the identity of the immediate electron donor to the photosynthetic reaction centre and with respect to the involvement of a cytochrome be complex in photo-induced electron transport of green sulphur bacteria.

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Purification of membrane‐bound cytochromes and a photoactive P840 protein complex of the green sulfur bacterium Chlorobium limicola f. thiosulfatophilum

Abstract: A photoactive P840 protein complex and a fraction enriched in cytochrome b from chromatophores of Chlorobzuzn lzmzcola f. thiosulfatophzlum are described. The former 1s identical in pigment composition to the 'core complex' of Prostecochlorzs aestuarzz [(1983

Cited by 94 publications

References 32 publications

Molecular Genetic Identification of a Pathway for Heme Binding to Cytochrome b 6

Molecular Genetic Identification of a Pathway for Heme Binding to Cytochrome b 6

Photosynthetic reaction center genes in green sulfur bacteria and in photosystem 1 are related.

Electron Transfer Towards the RCI‐Type Photosystem in the Green Sulphur Bacterium Chlorobium limicola Forma Thiosulphatophilum Studied by Time‐Resolved Optical Spectroscopy In Vivo

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