Related Experiment Video
Updated: Jul 7, 2026
08:04
A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
Cyanobacterial NDH-1 complexes: multiplicity in function and subunit composition.
Natalia Battchikova1, Eva-Mari Aro
1Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FI-20520 Turku, Finland. natbat@utu.fi
Physiologia Plantarum
|February 7, 2008
Summary
Cyanobacteria utilize NAD(P)H:quinone oxidoreductase (NDH-1) for respiration and CO2 uptake. This review details structural and functional differences between NDH-1L and NDH-1MS complexes, highlighting unanswered questions on their mechanisms.
Area of Science:
- Molecular Biology
- Biochemistry
- Photosynthesis Research
Background:
- NAD(P)H:quinone oxidoreductase (NDH-1) is crucial for cyanobacterial functions including respiration, cyclic electron flow around Photosystem I (PSI), and carbon dioxide (CO2) uptake.
- Diverse NDH-1 complexes with distinct structures and roles exist in cyanobacterial membranes.
Purpose of the Study:
- To review and compare the structural and functional characteristics of two primary cyanobacterial NDH-1 complexes: NDH-1L and NDH-1MS.
- To elucidate the roles of NDH-1L in respiration and PSI cyclic electron flow, and NDH-1MS in low-CO2 inducible CO2 uptake.
Main Methods:
- Review based on data from reverse genetics studies.
- Review based on data from proteomics studies.
Main Results:
- Cyanobacterial NDH-1 complexes share a common NDH-1M core.
- NDH-1L and NDH-1MS complexes differ in their distal membrane domains, comprising specific NdhD and NdhF proteins.
- NDH-1MS complexes involved in CO2 uptake are associated with a hydrophilic carbon uptake (CUP) domain.
Conclusions:
- Significant structural variations exist within cyanobacterial NDH-1 complexes, correlating with their specialized functions.
- Key questions remain regarding the identity of catalytically active subunits, substrate specificity, and reaction mechanisms of these complexes.
Related Concept Videos
01:43Electron Transport Chain: Complex III and IV
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
01:46Electron Transport Chain: Complex I and II
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
ROS generation is regulated and maintained at moderate levels necessary...
01:41The Supercomplexes in the Crista Membrane
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:30Bacterial Phylum Cyanobacteria
Cyanobacteria are a diverse group of oxygenic, phototrophic bacteria that played a pivotal role in converting Earth’s atmosphere from anoxic to oxygen-rich billions of years ago. They exhibit remarkable morphological diversity, ranging from unicellular forms to filamentous types, with cell sizes varying between 0.5 μm and 100 μm. Cyanobacteria are classified into five groups: Chroococcales (unicellular, dividing by binary fission), Pleurocapsales (unicellular, dividing by multiple fission),...
00:43Bacterial RNA Polymerase
Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...