A1 Refereed original research article in a scientific journal
Cyanobacterial NDH-1 complexes: multiplicity in function and subunit composition
Authors: Battchikova N, Aro EM
Publisher: BLACKWELL PUBLISHING
Publication year: 2007
Journal:: Physiologia Plantarum
Journal name in source: PHYSIOLOGIA PLANTARUM
Journal acronym: PHYSIOL PLANTARUM
Volume: 131
Issue: 1
First page : 22
Last page: 32
Number of pages: 11
ISSN: 0031-9317
DOI: https://doi.org/10.1111/j.1399-3054.2007.00929.x
Abstract
In cyanobacteria, the NAD(P)H:quinone oxicloreductase (NDH-1) is involved in a variety of functions like respiration, cyclic electron flow around PSI and CO2 uptake. Several types of NDH-1 complexes, which differ in structure and are responsible for these functions, exist in cyanobacterial membranes. This minireview is based on data obtained by reverse genetics and proteomics studies and focuses on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1 L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake. The NDH-1 complexes in cyanobacteria share a common NDH-1 M 'core' complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain. At present, however, very important questions concerning the nature of catalytically active subunits that constitute the electron input device (like NADH dehydrogenase module of the eubacterial 'model' NDH-1 analogs), the substrate specificity and reaction mechanisms of cyanobacterial complexes remain unanswered and are shortly discussed here.
In cyanobacteria, the NAD(P)H:quinone oxicloreductase (NDH-1) is involved in a variety of functions like respiration, cyclic electron flow around PSI and CO2 uptake. Several types of NDH-1 complexes, which differ in structure and are responsible for these functions, exist in cyanobacterial membranes. This minireview is based on data obtained by reverse genetics and proteomics studies and focuses on the structural and functional differences of the two types of cyanobacterial NDH-1 complexes: NDH-1 L, important for respiration and PSI cyclic electron flow, and NDH-1MS, the low-CO2 inducible complex participating in CO2 uptake. The NDH-1 complexes in cyanobacteria share a common NDH-1 M 'core' complex and differ in the composition of the distal membrane domain composed of specific NdhD and NdhF proteins, which in complexes involved in CO2 uptake is further associated with the hydrophilic carbon uptake (CUP) domain. At present, however, very important questions concerning the nature of catalytically active subunits that constitute the electron input device (like NADH dehydrogenase module of the eubacterial 'model' NDH-1 analogs), the substrate specificity and reaction mechanisms of cyanobacterial complexes remain unanswered and are shortly discussed here.
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