Asset Details
Do you wish to reserve the book?
Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase
Do you wish to request the book?
Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase
2020
Overview
NAD(P)H dehydrogenase-like (NDH) complex NDH-1L of cyanobacteria plays a crucial role in cyclic electron flow (CEF) around photosystem I and respiration processes. NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen that drives the ATP production. NDH-1L-dependent CEF increases the ATP/NADPH ratio, and is therefore pivotal for oxygenic phototrophs to function under stress. Here we report two structures of NDH-1L from
Thermosynechococcus elongatus
BP-1, in complex with one Fd and an endogenous PQ, respectively. Our structures represent the complete model of cyanobacterial NDH-1L, revealing the binding manner of NDH-1L with Fd and PQ, as well as the structural elements crucial for proper functioning of the NDH-1L complex. Together, our data provides deep insights into the electron transport from Fd to PQ, and its coupling with proton translocation in NDH-1L.
NAD(P)H dehydrogenase-like complex NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen. Here authors report two structures of NDH-1L from
Thermosynechococcus elongatus
BP-1, in complex with one Fd and an endogenous PQ, respectively.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/103
/ 82/80
/ 82/83
/ Couples
/ Electron Transport Complex I - chemistry
/ Electron Transport Complex I - ultrastructure
/ Humanities and Social Sciences
/ Hydrophobic and Hydrophilic Interactions
/ NAD
/ NADP
/ NADPH Dehydrogenase - chemistry
/ NADPH Dehydrogenase - ultrastructure
/ Protein Subunits - chemistry
/ Protons
/ Pumping
/ Science
/ Structural Homology, Protein
