2011
DOI: 10.1016/j.febslet.2011.08.035
|View full text |Cite
|
Sign up to set email alerts
|

The cytochrome f–plastocyanin complex as a model to study transient interactions between redox proteins

Abstract: Transient complexes, with a lifetime ranging between microseconds and seconds, are essential for biochemical reactions requiring a fast turnover. That is the case of the interactions between proteins engaged in electron transfer reactions, which are involved in relevant physiological processes such as respiration and photosynthesis. In the latter, the copper protein plastocyanin acts as a soluble carrier transferring electrons between the two membrane‐embedded complexes cytochrome b 6 f and photosyst… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

2
19
0

Year Published

2012
2012
2022
2022

Publication Types

Select...
5
3
2

Relationship

1
9

Authors

Journals

citations
Cited by 33 publications
(22 citation statements)
references
References 53 publications
2
19
0
Order By: Relevance
“…The phenomenon of co-expression was also observed in miR398- plastocyanin , in which the expression levels of both miR398 and plastocyanin were higher in germinated embryos than in dormant embryos. Plastocyanin functions as a soluble carrier transferring electrons between cytochrome b(6)f and photosystem I [60]. The expression pattern of plastocyanin was consistent with the phenomenon that genes involved in photosynthesis and carbon fixation are upregulated from dormant embryos compared to germinated embryos [61].…”
Section: Discussionsupporting
confidence: 74%
“…The phenomenon of co-expression was also observed in miR398- plastocyanin , in which the expression levels of both miR398 and plastocyanin were higher in germinated embryos than in dormant embryos. Plastocyanin functions as a soluble carrier transferring electrons between cytochrome b(6)f and photosystem I [60]. The expression pattern of plastocyanin was consistent with the phenomenon that genes involved in photosynthesis and carbon fixation are upregulated from dormant embryos compared to germinated embryos [61].…”
Section: Discussionsupporting
confidence: 74%
“…These differences arise from the experimental crystallographic data usually being recorded at a low temperature (77 K), thereby reducing the dynamics of the protein. A similar example is found in electron transfer complexes, for which the observation of specific salt bridges through molecular dynamic computations [ 46 , 60 ] explained the discrepancies between kinetic analyses of site-directed mutants [ 61 ] and structural data [ 62 ].…”
Section: Discussionmentioning
confidence: 74%
“…The role of electrostatic interactions in the formation of the oxidation-reduction complex of two proteins was studied in the interaction model of the well-studied pair of photosynthetic electron transfer proteins, Pc and Cyt f. This pair of proteins is a classic object of experimental research (reviewed by Cruz-Gallardo et al [25], and Khruschev et al [12]) and Brownian dynamics studies [13,18,23,24,[26][27][28][29]. The physiological function of the protein Pc consists of the shuttle electron transfer between the subunit f of cytochrome complex b6-f and the photosystem I in all higher plants and some algae.…”
Section: Productive and Non-productive Encounter Complexesmentioning
confidence: 99%