Some observations on the primary acceptor of <i>Rhodopseudomonas viridis</i>

Cogdell, Richard J.; Crofts, Antony R.

doi:10.1016/0014-5793(72)80435-6

Cited by 31 publications

(12 citation statements)

References 11 publications

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“…viridis as compared with Rb. sphaeroides as measured by redox titration (Cogdell and Crofts, 1972;Prince and Dutton, 1978;Rutherford et al, 1979). From the equilibrium constants, the Em of QB/QB" would be expected to be similar for the two.…”

Section: Biophysical Analyses?differencesmentioning

confidence: 99%

Expression of a Higher Plant psbA Gene in Synechocystis 6803 Yields a Functional Hybrid Photosystem II Reaction Center Complex

Nixon¹,

Rögner²,

Diner³

1991

The Plant Cell

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The psbA gene codes for the D1 polypeptide of the photosystem II reaction center complex and is found in all photosynthetic organisms that carry out oxygenic photosynthesis. Here we describe the construction and characterization of a strain of the cyanobacterium Synechocystis sp PCC 6803 in which the three endogenous psbA genes are replaced by a single psbA gene from the chloroplast genome of the higher plant Poa annua. The resulting chimeric strain, KWPAS, grows photoautotrophically with a doubling time of 26 hours compared with 20 hours for wild-type Synechocystis 6803. The mutant oxidizes water to oxygen at light-saturated rates comparable with wild type, despite differences in 15% of the primary structure of D1 between these species. RNA gel blot analysis indicates the presence in KWPAS of a psbA transcript of approximately 1.25 kilobases, consistent with the chloroplast promoter also acting as a promoter in Synechocystis. By using antibodies specific for the carboxyl-terminal extension of the D1 polypeptide of higher plants, we showed that the D1 polypeptide synthesized by KWPAS is post-translationally modified at the carboxyl terminus, probably through processing. A detailed biophysical analysis of the chimeric photosystem II complex indicated that the rates of forward electron transfer are similar to wild type. The rates of charge recombination between the donor and acceptor sides of the reaction center are, however, accelerated by as much as a factor of nine (QA- to S2) and are the most likely explanation for the lower rate of photoautotrophic growth in the mutant. We conclude that the psbA gene from a higher plant can be expressed in cyanobacteria and its product processed and assembled into a functional chimeric photosystem II reaction center.

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Section: Biophysical Analyses?differencesmentioning

confidence: 99%

Expression of a Higher Plant psbA Gene in Synechocystis 6803 Yields a Functional Hybrid Photosystem II Reaction Center Complex

Nixon¹,

Rögner²,

Diner³

1991

The Plant Cell

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“…viridis as compared with Rb. sphaeroides as measured by redox titration (Cogdell and Crofts, 1972;Prince and Dutton, 1978;Rutherford et al, 1979). From the equilibrium constants, the E , of QB/QB-would be expected to be similar for the two.…”

Section: Biophysical Analyses-differencesmentioning

confidence: 99%

Expression of a higher plant psbA gene in Synechocystis 6803 yields a functional hybrid photosystem II reaction center complex.

1991

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The psbA gene codes for the D1 polypeptide of the photosystem I 1 reaction center complex and is found in a11 photosynthetic organisms that carry out oxygenic photosynthesis. Here we describe the construction and characterization of a strain of the cyanobacterium Synechocystis sp PCC 6803 in which the three endogenous psbA genes are replaced by a single psbA gene from the chloroplast genome of the higher plant Poa annua. The resulting chimeric strain, KWPAS, grows photoautotrophically with a doubling time of 26 hours compared with 20 hours for wild-type Synechocystis 6803. The mutant oxidizes water to oxygen at light-saturated rates comparable with wild type, despite differences in 15% of the primary structure of D1 between these species. RNA gel blot analysis indicates the presence in KWPAS of a psbA transcript of approximately 1.25 kilobases, consistent with the chloroplast promoter also acting as a promoter in Synechocystis. By using antibodies specific for the carboxyl-terminal extension of the D1 polypeptide of higher plants, we showed that the D1 polypeptide synthesized by KWPAS is posttranslationally modified at the carboxyl terminus, probably through processing. A detailed biophysical analysis of the chimeric photosystem I 1 complex indicated that the rates of forward electron transfer are similar to wild type. The rates of charge recombination between the donor and acceptor sides of the reaction center are, however, accelerated by as much as a factor of nine (QA-to S p ) and are the most likely explanation for the lower rate of photoautotrophic growth in the mutant. We conclude that the psbA gene from a higher plant can be expressed in cyanobacteria and its product processed and assembled into a functional chimeric photosystem I 1 reaction center.

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“…The redox potential of BP/BPis intermediate with about -400 mV (Cogdell and Crofts, 1972;Carithers and Parson, 1975;Prince et al, 1976;Netzel et al, 1977;Bolton, 1978;Holten et al, 1978;Woodbury et al, 1985;Breton et al, 1986). The redox potential of BP/BPis intermediate with about -400 mV (Cogdell and Crofts, 1972;Carithers and Parson, 1975;Prince et al, 1976;Netzel et al, 1977;Bolton, 1978;Holten et al, 1978;Woodbury et al, 1985;Breton et al, 1986).…”

Section: The Protein As a Polydentate Ligandmentioning

confidence: 99%

A Structural Basis of Light Energy and Electron Transfer in Biology (Nobel Lecture)

Huber

1989

Angew. Chem. Int. Ed. Engl.

262

117

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Aspects of intramolecular light energy and electron transfer will be discussed for three protein‐‐cofactor complexes, whose three‐dimensional structures have been elucidated by X‐ray crystallography: components of light‐harvesting cyanobacterial phycobilisomes; the purple bacterial reaction centre; and the blue multi‐copper oxidases. A wealth of functional data is available for these systems which allows specific correlations between structure and function and general conclusions about light energy and electron transfer in biological materials to be made.

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Some observations on the primary acceptor of Rhodopseudomonas viridis

Cited by 31 publications

References 11 publications

Expression of a Higher Plant psbA Gene in Synechocystis 6803 Yields a Functional Hybrid Photosystem II Reaction Center Complex

Expression of a Higher Plant psbA Gene in Synechocystis 6803 Yields a Functional Hybrid Photosystem II Reaction Center Complex

Expression of a higher plant psbA gene in Synechocystis 6803 yields a functional hybrid photosystem II reaction center complex.

A Structural Basis of Light Energy and Electron Transfer in Biology (Nobel Lecture)

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