Function of three cytochromes in photosynthesis of whole cells of Rhodospirillum rubrum as studied by flash spectroscopy. Evidence for two types of reaction center

Grondelle, Rienk van; Duysens, L.N.M.; Wal, H. N. Van Der

doi:10.1016/0005-2728(76)90131-6

Cited by 50 publications

(11 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Picorel and co-workers (181) suggest that this mutant may be enriched in a second kind of reaction center which does not contain P800 and which is present as a minor component in wild-type cells. Such an explanation would reinforce previous proposals (236,256) that two different kinds of reaction center coexist in membranes of R. rubrum. Alternatively, the reaction center of strain F24.1 may be modified so as to render P800 unnecessary.…”

Section: Survey Of Mutants Of the Rhodospirillaceaesupporting

confidence: 86%

Genetics of Rhodospirillaceae.

Saunders¹

1978

Microbiological Reviews

View full text Add to dashboard Cite

Section: Survey Of Mutants Of the Rhodospirillaceaesupporting

confidence: 86%

Genetics of Rhodospirillaceae.

Saunders¹

1978

Microbiological Reviews

View full text Add to dashboard Cite

“…litoralis also does not possess a cyt c tightly bound to RC. However, the time-resolved photochemistry of this species was different from that of E. longus, E. ramosum, E. hydrolyticum, and E. ezovicum, reminiscent of that described for the anaerobic purple nonsulfur species R. rubrum (185). A light-induced difference spectrum detected at 50 s indicates photooxidation of the RC primary donor, and complete cyt c oxidation was observed only after 10 ms (Fig.…”

Section: Photosynthetic Electron Transfermentioning

confidence: 74%

Aerobic Anoxygenic Phototrophic Bacteria

Yurkov

Beatty

1998

Microbiol Mol Biol Rev

429

241

View full text Add to dashboard Cite

SUMMARY The aerobic anoxygenic phototrophic bacteria are a relatively recently discovered bacterial group. Although taxonomically and phylogenetically heterogeneous, these bacteria share the following distinguishing features: the presence of bacteriochlorophyll a incorporated into reaction center and light-harvesting complexes, low levels of the photosynthetic unit in cells, an abundance of carotenoids, a strong inhibition by light of bacteriochlorophyll synthesis, and the inability to grow photosynthetically under anaerobic conditions. Aerobic anoxygenic phototrophic bacteria are classified in two marine (Erythrobacter and Roseobacter) and six freshwater (Acidiphilium, Erythromicrobium, Erythromonas, Porphyrobacter, Roseococcus, and Sandaracinobacter) genera, which phylogenetically belong to the α-1, α-3, and α-4 subclasses of the class Proteobacteria. Despite this phylogenetic information, the evolution and ancestry of their photosynthetic properties are unclear. We discuss several current proposals for the evolutionary origin of aerobic phototrophic bacteria. The closest phylogenetic relatives of aerobic phototrophic bacteria include facultatively anaerobic purple nonsulfur phototrophic bacteria. Since these two bacterial groups share many properties, yet have significant differences, we compare and contrast their physiology, with an emphasis on morphology and photosynthetic and other metabolic processes.

show abstract

“…On the other hand, van Grondelle and coworkers showed that functionally similar cytochromes in Rhodospirillum rubrum (cytochrome c420) [17] and Chromatium vinosum (cytochrome Cssl) [18] were mobile, and this was supported by the light saturation characteristics of cytochrome oxidation in a short flash [19]. A similar analysis in Rp.…”

Section: Introductionmentioning

confidence: 98%

Photooxidation of mitochondrial cytochrome c by isolated bacterial reaction centers: Evidence for tight-binding and diffusional pathways

Overfield

Wraight

1986

Photosynth Res

View full text Add to dashboard Cite

The binding of horse heart mitochondrial cytochrome c to isolated reaction centers from Rhodopseudomonas sphaeroides is described. The kinetics of photooxidation of cytochrome c following a short actinic flash is compared to the expected binding state of the cytochrome at various concentrations and at different ionic strengths. At low ionic strength a very tight binding site (KD≦10(-8) M) is apparent which is nonfunctional with respect to electron donation to the bound reaction center. This tightly bound cytochrome can react with another reaction center in a diffusion limited, second order process. A weaker binding site (KD≃0.3 · 10(-6) M) is also boserved which is associated with rapid, first order electron transfer from cytochrome to reaction center. Both binding processes are weakened in the presence of salt and there is no detectable binding in 100 mM NaCl. Under such conditions cytochrome oxidation is entirely a diffusional, second order process. However, analysis of the flash intensity dependence of the extent of cytochrome oxidation, by the method of van Grondelle (van Grondelle, R. (1978) Ph.D. Thesis, State University, Leiden) indicated that the cytochrome was not freely mobile even in 100 mM NaCl, at least in the sense that reduced cytochrome only slowly dissociates from unactivated reaction centers. An overall kinetic/equilibrium scheme for cytochrome c binding and photooxidation by reaction centers is presented. This is very similar to that described earlier for cytochrome c2 (Overfield, R.E., Wraight, C.A. and DeVault, D. (1979) FEBS Lett. 105, 137-142), but the tight binding site and associated diffusion controlled oxidation is unique to cytochrome c.

show abstract

Function of three cytochromes in photosynthesis of whole cells of Rhodospirillum rubrum as studied by flash spectroscopy. Evidence for two types of reaction center

Cited by 50 publications

References 36 publications

Genetics of Rhodospirillaceae.

Genetics of Rhodospirillaceae.

Aerobic Anoxygenic Phototrophic Bacteria

Photooxidation of mitochondrial cytochrome c by isolated bacterial reaction centers: Evidence for tight-binding and diffusional pathways

Contact Info

Product

Resources

About