An isolated reaction center complex from the green sulfur bacterium Chlorobium vibrioforme can photoreduce ferredoxin at high rates

Kjær, Bodil; Scheller, Henrik Vibe

doi:10.1007/bf00017751

Cited by 25 publications

(3 citation statements)

References 30 publications

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“…2B ). The E m value of +217 mV obtained for the WT RC is close to the values reported previously 35 36 37 . The L688C and V689C mutations similarly upshifted the E m by about 30 mV, resulting in values of +251 mV and +247 mV, respectively ( Table 1 ).…”

Section: Resultssupporting

confidence: 90%

Mutation-induced perturbation of the special pair P840 in the homodimeric reaction center in green sulfur bacteria

Azai

Sano

Kato

et al. 2016

Sci Rep

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Homodimeric photosynthetic reaction centers (RCs) in green sulfur bacteria and heliobacteria are functional homologs of Photosystem (PS) I in oxygenic phototrophs. They show unique features in their electron transfer reactions; however, detailed structural information has not been available so far. We mutated PscA-Leu688 and PscA-Val689 to cysteine residues in the green sulfur bacterium Chlorobaculum tepidum; these residues were predicted to interact with the special pair P840, based on sequence comparison with PS I. Spectroelectrochemical measurements showed that the L688C and V689C mutations altered a near-infrared difference spectrum upon P840 oxidation, as well as the redox potential of P840. Light-induced Fourier transform infrared difference measurements showed that the L688C mutation induced a differential signal of the S-H stretching vibration in the P840+/P840 spectrum, as reported in P800+/P800 difference spectrum in a heliobacterial RC. Spectral changes in the 131-keto C=O region, caused by both mutations, revealed corresponding changes in the electronic structure of P840 and in the hydrogen-bonding interaction at the 131-keto C=O group. These results suggest that there is a common spatial configuration around the special pair sites among type 1 RCs. The data also provided evidence that P840 has a symmetric electronic structure, as expected from a homodimeric RC.

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Section: Resultssupporting

confidence: 90%

Mutation-induced perturbation of the special pair P840 in the homodimeric reaction center in green sulfur bacteria

Azai

Sano

Kato

et al. 2016

Sci Rep

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“…The E m values of P840, cyt c z and the Rieske center were reported to be +230 to +240, +170 to +180 mV (or +188 mV as determined as an isolated protein), and +130 to +150 mV, respectively ( Okumura et al, 1994 ; Kjær and Scheller, 1996 ; Hirano et al, 2010 ; Knaff and Malkin, 1976 ). That of cyt c -556 was presently determined to be +190 mV (see Fig.…”

Section: Resultsmentioning

confidence: 99%

Soluble domains of cytochrome c-556 and Rieske iron–sulfur protein from Chlorobaculum tepidum: Crystal structures and interaction analysis

Kishimoto¹,

Azai²,

Yamamoto³

et al. 2023

Current Research in Structural Biology

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“…The NADP + photoreduction activity was determined as described in Naver et al. (1999) and Kjær and Scheller (1996).…”

Section: Methodsmentioning

confidence: 99%

AtCYP38 ensures early biogenesis, correct assembly and sustenance of photosystem II

et al. 2008

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SummaryAtCYP38 is a thylakoid lumen protein comprising the immunophilin domain and the phosphatase inhibitor module. Here we show the association of AtCYP38 with the photosystem II (PSII) monomer complex and address its functional role using AtCYP38-deficient mutants. The dynamic greening process of etiolated leaves failed in the absence of AtCYP38, due to specific problems in the biogenesis of PSII complexes. Also the development of leaves under short-day conditions was severely disturbed. Detailed biophysical and biochemical analysis of mature AtCYP38-deficient plants from favorable growth conditions (long photoperiod) revealed: (i) intrinsic malfunction of PSII, which (ii) occurred on the donor side of PSII and (iii) was dependent on growing light intensity. AtCYP38 mutant plants also showed decreased accumulation of PSII, which was shown not to originate from impaired D1 synthesis or assembly of PSII monomers, dimers and supercomplexes as such but rather from the incorrect fine-tuning of the oxygen-evolving side of PSII. This, in turn, rendered PSII centers extremely susceptible to photoinhibition. AtCYP38 deficiency also drastically decreased the in vivo phosphorylation of PSII core proteins, probably related to the absence of the AtCYP38 phosphatase inhibitor domain. It is proposed that during PSII assembly AtCYP38 protein guides the proper folding of D1 (and CP43) into PSII, thereby enabling the correct assembly of the water-splitting Mn 4 -Ca cluster even with high turnover of PSII.

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An isolated reaction center complex from the green sulfur bacterium Chlorobium vibrioforme can photoreduce ferredoxin at high rates

Cited by 25 publications

References 30 publications

Mutation-induced perturbation of the special pair P840 in the homodimeric reaction center in green sulfur bacteria

Mutation-induced perturbation of the special pair P840 in the homodimeric reaction center in green sulfur bacteria

Soluble domains of cytochrome c-556 and Rieske iron–sulfur protein from Chlorobaculum tepidum: Crystal structures and interaction analysis

AtCYP38 ensures early biogenesis, correct assembly and sustenance of photosystem II

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