Structural insights into NDH-1 mediated cyclic electron transfer

Zhang, Chunli; Jin, Shu‐Guang; Ran, Zhaoxing; Zhao, Jing–Shan; Wu, Zhenfang; Liao, Rijing; Wu, Jian; Ma, Weimin; Lei, Ming

doi:10.1038/s41467-020-14732-z

Cited by 61 publications

(78 citation statements)

References 77 publications

(116 reference statements)

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“…The chloroplast complex resembles that of cyanobacteria, which transfers electrons from ferredoxin to plastoquinone. The high-resolution structure of cyanobacterial complex I has recently been resolved by cryoEM (Laughlin et al, 2019; Schuller et al, 2019; Zhang et al, 2020). The structure of plant mitochondrial complex I is less well characterized.…”

Section: Introductionmentioning

confidence: 99%

A ferredoxin bridge connects the two arms of plant mitochondrial complex I

Klusch

Senkler

Yıldız

et al. 2020

Preprint

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SUMMARYMitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. It is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and from the green alga Polytomella sp. at 3.2 and 3.3 Å resolution. In both, a heterotrimeric γ-carbonic anhydrase domain is attached to the membrane arm on the matrix side. Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 loop near the quinol binding site. The angle appears to depend on a bridge domain, which links the peripheral arm to the membrane arm and includes an unusual ferredoxin. We suggest that the bridge domain regulates complex I activity.One sentence summaryThe activity of complex I depends on the angel between its two arms, which, in plants, is adjusted by a protein bridge that includes an unusual ferredoxin.The authors responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantcell.org) are: Hans-Peter Braun (braun@genetik.uni-hannover.de) and Werner Kühlbrandt (werner.kuehlbrandt@biophys.mpg.de).

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Section: Introductionmentioning

confidence: 99%

A ferredoxin bridge connects the two arms of plant mitochondrial complex I

Klusch

Senkler

Yıldız

et al. 2020

Preprint

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“…M55, on the other hand, was relatively unaffected by the addition of KCN. As well, the characteristic post-illumination fluorescence rise associated with NDH-1 activity [7,23,41,60] was observed in both the WT and ΔndhF1, with its magnitude being enhanced by the addition of KCN, though to a much greater degree in the WT both with and without KCN. M55 had no rise in either condition.…”

Section: Ndh-11/2 Complexes Are Largely Responsible For Ndh-1 Driven mentioning

confidence: 74%

“…NADH dehydrogenase complex I, or complex I, is a widely distributed bioenergetic complex, with homologs seen in archaea, bacteria, and eukaryotes [1]. The core structure of these complexes and their subunit composition have been largely conserved throughout these phyletic kingdoms, with the bacterial complexes possessing the fewest subunits, and eukaryotes possessing accessory subunits, but retaining a core that is conserved across the domains of life [2][3][4][5][6][7]. These complexes are vital parts of a diverse variety of electron transport chains and have been shown to couple proton pumping to electron transport from ferredoxin (Fd) or NAD(P)H to a quinone to increase the proton motive force (PMF) for ATP production in heterotrophic bacteria as well as mitochondria and chloroplasts [3,[8][9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

“…Cyanobacteria also possess complex I, however they are unique in possessing four functional versions of complex I, and they are termed NDH-1 for NADPH Dehydrogenase 1 complex, though they have recently been shown to utilize Fd for their reductant over NADPH [7,19,20]. Recently, the structure of two cyanobacterial NDH-1 complexes have been solved [4][5][6][7], covering representatives of the major functions of these complexes: Cyclic electron flow (CEF), respiratory electron flow, and CO2 uptake. A summary of the components of photosynthetic electron flow, their actions on proton pumping, and inhibitors utilized here are shown in Fig.…”

Section: Introductionmentioning

confidence: 99%

“…This accelerated consumption of electrons is thought to act as an antioxidant mechanism in this way, especially 8 when stresses such as high light leads to increased Fd reduction. Recently, it was shown that exposure to high light caused heavy accumulation of the NDH-13/4 complexes, indicating their CO2 uptake activity in addition to their CEF activity may play a role in the NDH-1 antioxidant mechanism [7]. The deletion of the NDH-11/2 complexes causes a hyper-oxidation of the PQ pool, locking the photosynthetic machinery in State 1 where the bulk of light harvesting is focused around PSII [34,35].…”

Section: Introductionmentioning

confidence: 99%

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Electron flow through NDH-1 complexes is the major driver of cyclic electron flow-dependent proton pumping in cyanobacteria

Miller

Vaughn²,

Burnap

2020

Preprint

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Cyclic electron flow (CEF) around Photosystem I is vital to balancing the photosynthetic energy budget of cyanobacteria and other photosynthetic organisms. The coupling of CEF to proton pumping has long been hypothesized to occur, providing proton motive force (PMF) for the synthesis of ATP with no net cost to [NADPH]. This is thought to occur largely through the activity of NDH-1 complexes, of which cyanobacteria have four with different activities. While a much work has been done to understand the steady-state PMF in both the light and dark, and fluorescent probes have been developed to observe these fluxes in vivo, little has been done to understand the kinetics of these fluxes, particularly with regard to NDH-1 complexes. To monitor the kinetics of proton pumping in Synechocystis sp. PCC 6803, the pH sensitive dye Acridine Orange was used alongside a suite of inhibitors in order to observe light-dependent proton pumping. The assay was demonstrated to measure photosynthetically driven proton pumping and used to measure the rates of proton pumping unimpeded by dark ΔpH. Here, the cyanobacterial NDH-1 complexes are shown to pump a sizable portion of proton flux when CEF-driven and LEF-driven proton pumping rates are observed and compared in mutants lacking some or all NDH-1 complexes. It is also demonstrated that PSII and LEF are responsible for the bulk of light induced proton pumping, though CEF and NDH-1 are capable of generating ~40% of the proton pumping rate when LEF is inactivated.

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NDH‐1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria

et al. 2023

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Cyanobacterial NdhM, an oxygenic photosynthesis‐specific NDH‐1 subunit, has been found to be essential for the formation of a large complex of NDH‐1 (NDH‐1L). The cryo‐electron microscopic (cryo‐EM) structure of NdhM from Thermosynechococcus elongatus showed that the N‐terminus of NdhM contains three β‐sheets, while two α‐helixes are present in the middle and C‐terminal part of NdhM. Here, we obtained a mutant of the unicellular cyanobacterium Synechocystis 6803 expressing a C‐terminal truncated NdhM subunit designated NdhMΔC. Accumulation and activity of NDH‐1 were not affected in NdhMΔC under normal growth conditions. However, the NDH‐1 complex with truncated NdhM is unstable under stress. Immunoblot analyses showed that the assembly process of the cyanobacterial NDH‐1L hydrophilic arm was not affected in the NdhMΔC mutant even under high temperature. Thus, our results indicate that NdhM can bind to the NDH‐1 complex without its C‐terminal α‐helix, but the interaction is weakened. NDH‐1L with truncated NdhM is more prone to dissociation, and this is particularly evident under stress conditions.

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Structural insights into NDH-1 mediated cyclic electron transfer

Cited by 61 publications

References 77 publications

A ferredoxin bridge connects the two arms of plant mitochondrial complex I

A ferredoxin bridge connects the two arms of plant mitochondrial complex I

Electron flow through NDH-1 complexes is the major driver of cyclic electron flow-dependent proton pumping in cyanobacteria

NDH‐1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria

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