title: Bacterial Electron Transfer Chains Primed by Proteomics.
abstract: Electron transport phosphorylation is the central mechanism for most prokaryotic species to harvest energy released in the respiration of their substrates as ATP. Microorganisms have evolved incredible variations on this principle, most of these we perhaps do not know, considering that only a fraction of the microbial richness is known. Besides these variations, microbial species may show substantial versatility in using respiratory systems. In connection herewith, regulatory mechanisms control the expression of these respiratory enzyme systems and their assembly at the translational and posttranslational levels, to optimally accommodate changes in the supply of their energy substrates. Here, we present an overview of methods and techniques from the field of proteomics to explore bacterial electron transfer chains and their regulation at levels ranging from the whole organism down to the Ångstrom scales of protein structures. From the survey of the literature on this subject, it is concluded that proteomics, indeed, has substantially contributed to our comprehending of bacterial respiratory mechanisms, often in elegant combinations with genetic and biochemical approaches. However, we also note that advanced proteomics offers a wealth of opportunities, which have not been exploited at all, or at best underexploited in hypothesis-driving and hypothesis-driven research on bacterial bioenergetics. Examples obtained from the related area of mitochondrial oxidative phosphorylation research, where the application of advanced proteomics is more common, may illustrate these opportunities.
authors.affiliation: Nijmegen Center for Mitochondrial Disorders, Radboud Proteomics Centre, Translational Metabolic Laboratory, Radboud University Medical Center, Nijmegen, The Netherlands.
authors.forename: H J C T
authors.initials: HJ
authors.lastname: Wessels
authors.affiliation: Institute of Water and Wetland Research, Radboud University Nijmegen, Nijmegen, The Netherlands.
authors.forename: N M
authors.initials: NM
authors.lastname: de Almeida
authors.affiliation: Institute of Water and Wetland Research, Radboud University Nijmegen, Nijmegen, The Netherlands; Laboratory of Microbiology, Ghent University, Ghent, Belgium.
authors.forename: B
authors.initials: B
authors.lastname: Kartal
authors.affiliation: Institute of Water and Wetland Research, Radboud University Nijmegen, Nijmegen, The Netherlands. Electronic address: j.keltjens@science.ru.nl.
authors.forename: J T
authors.initials: JT
authors.lastname: Keltjens
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001419:Bacteria / Q000378:metabolism*; D004579:Electron Transport; D042967:Electron Transport Complex I / Q000648:ultrastructure*; D042963:Electron Transport Complex II / Q000648:ultrastructure*; D010084:Oxidation-Reduction; D010085:Oxidative Phosphorylation; D018384:Oxidative Stress / Q000502:physiology; D010100:Oxygen / Q000378:metabolism; D010766:Phosphorylation / Q000502:physiology; D011499:Protein Processing, Post-Translational / Q000502:physiology; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods*
chemical_list: D000255:Adenosine Triphosphate; D042963:Electron Transport Complex II; D042967:Electron Transport Complex I; D010100:Oxygen
keywords: Anammox bacteria; Differential expression; Methanothermobacter thermautotrophicus; Mitochondria; Proteomics; Respiratory complexes