Electrocatalytic evidence of the diversity of the oxygen reaction in the bacterial bd oxidase from different organisms

Nikolaev, Anton; Safarian, Schara; Thesseling, Alexander; Wohlwend, Daniel; Friedrich, Thorsten; Michel, Hartmut; Kusumoto, Tomoichirou; Sakamoto, Junshi; Melin, Frédéric; Hellwig, Petra

doi:10.1016/j.bbabio.2021.148436

Cited by 7 publications

(19 citation statements)

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“…Taken together, the redox potentials of the bd-II cofactors are 60-80 mV (b-type hemes) and 180 mV (heme d) more positive than those of the corresponding cofactors in bd-I (Fig. 1) 30 .…”

Section: Resultsmentioning

confidence: 78%

Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D

Kägi

Grauel

Rasmussen

et al. 2022

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…Taken together, the redox potentials of the bd-II cofactors are 60-80 mV (b-type hemes) and 180 mV (heme d) more positive than those of the corresponding cofactors in bd-I (Fig. 1) 30 .…”

Section: Resultsmentioning

confidence: 78%

Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D

Kägi

Grauel

Rasmussen

et al. 2022

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…In contrast to the electron transport chain of mammals that is unbranched, E. coli , like many other prokaryotes, possesses the branched aerobic respiratory chain ( Figure 7 ) [ 45 , 97 , 98 , 99 , 100 , 101 , 102 ]. The E. coli chain comprises of type I and type II NADH dehydrogenases which transfer electrons from NADH to ubiquinol-8 (UQ8) or menaquinol-8 (MQ8); succinate dehydrogenase transferring electrons from succinate to UQ8; and three terminal oxidases, cytochromes bo 3 , bd -I, and bd -II which transfer electrons from UQ8 or MQ8 to O 2 producing H 2 O [ 103 , 104 , 105 , 106 , 107 , 108 , 109 , 110 , 111 , 112 ]. The proton motive force generated by type I NADH dehydrogenase and the terminal oxidases is used by F o F 1 -ATP synthase to make ATP [ 113 , 114 , 115 ].…”

Section: Effect Of H 2 S On the Operation Of The Branched Respiratory Chain Of E Coli And Bacterialmentioning

confidence: 99%

Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics

Borisov

Forte

2021

IJMS

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This review focuses on the effects of hydrogen sulfide (H2S) on the unique bioenergetic molecular machines in mitochondria and bacteria—the protein complexes of electron transport chains and associated enzymes. H2S, along with nitric oxide and carbon monoxide, belongs to the class of endogenous gaseous signaling molecules. This compound plays critical roles in physiology and pathophysiology. Enzymes implicated in H2S metabolism and physiological actions are promising targets for novel pharmaceutical agents. The biological effects of H2S are biphasic, changing from cytoprotection to cytotoxicity through increasing the compound concentration. In mammals, H2S enhances the activity of FoF1-ATP (adenosine triphosphate) synthase and lactate dehydrogenase via their S-sulfhydration, thereby stimulating mitochondrial electron transport. H2S serves as an electron donor for the mitochondrial respiratory chain via sulfide quinone oxidoreductase and cytochrome c oxidase at low H2S levels. The latter enzyme is inhibited by high H2S concentrations, resulting in the reversible inhibition of electron transport and ATP production in mitochondria. In the branched respiratory chain of Escherichia coli, H2S inhibits the bo3 terminal oxidase but does not affect the alternative bd-type oxidases. Thus, in E. coli and presumably other bacteria, cytochrome bd permits respiration and cell growth in H2S-rich environments. A complete picture of the impact of H2S on bioenergetics is lacking, but this field is fast-moving, and active ongoing research on this topic will likely shed light on additional, yet unknown biological effects.

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“…Canonical cytochrome bd oxidases share a common core architecture of two subunits, denoted CydA and CydB, which may be accompanied by up to two additional single-transmembrane helix subunits (Miller and Gennis, 1983;VanOrsdel et al, 2013;Hoeser et al, 2014;Safarian et al, 2016;Safarian et al, 2019;Theßeling et al, 2019;Grund et al, 2021;Safarian et al, 2021;Wang et al, 2021;Friedrich et al, 2022). As implied by designation, cytochromes bd contain two b-type hemes (low-spin b 558 , high-spin b 595 ) and one d-type heme involved in quinol oxidation, electron transfer and oxygen reduction.…”

Section: Introductionmentioning

confidence: 99%

“…We previously reported X-ray and cryoEM structures of cytochrome bd oxidases from Geobacillus thermodenitrificans (3.8 Å), Escherichia coli (2.7 Å bd-I, 2.1 Å bd-II), and Mycobacterium tuberculosis (2.6 Å) (Safarian et al, 2016;Safarian et al, 2019;Grund et al, 2021;Safarian et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

The cryoEM structure of cytochrome bd from C. glutamicum provides novel insights into structural properties of actinobacterial terminal oxidases

et al. 2023

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Cytochromes bd are essential for microaerobic respiration of many prokaryotes including a number of human pathogens. These enzymes catalyze the reduction of molecular oxygen to water using quinols as electron donors. Their importance for prokaryotic survival and the absence of eukaryotic homologs make these enzyme ideal targets for antimicrobial drugs. Here, we determined the cryoEM structure of the menaquinol-oxidizing cytochrome bd-type oxygen reductase of the facultative anaerobic Actinobacterium Corynebacterium glutamicum at a resolution of 2.7 Å. The obtained structure adopts the signature pseudosymmetrical heterodimeric architecture of canonical cytochrome bd oxidases formed by the core subunits CydA and CydB. No accessory subunits were identified for this cytochrome bd homolog. The two b-type hemes and the oxygen binding heme d are organized in a triangular geometry with a protein environment around these redox cofactors similar to that of the closely related cytochrome bd from M. tuberculosis. We identified oxygen and a proton conducting channels emerging from the membrane space and the cytoplasm, respectively. Compared to the prototypical enzyme homolog from the E. coli, the most apparent difference is found in the location and size of the proton channel entry site. In canonical cytochrome bd oxidases quinol oxidation occurs at the highly flexible periplasmic Q-loop located in the loop region between TMHs six and seven. An alternative quinol-binding site near heme b595 was previously identified for cytochrome bd from M. tuberculosis. We discuss the relevance of the two quinol oxidation sites in actinobacterial bd-type oxidases and highlight important differences that may explain functional and electrochemical differences between C. glutamicum and M. tuberculosis. This study expands our current understanding of the structural diversity of actinobacterial and proteobacterial cytochrome bd oxygen reductases and provides deeper insights into the unique structural and functional properties of various cytochrome bd variants from different phylae.

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Electrocatalytic evidence of the diversity of the oxygen reaction in the bacterial bd oxidase from different organisms

Cited by 7 publications

References 50 publications

Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D

Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D

Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics

The cryoEM structure of cytochrome bd from C. glutamicum provides novel insights into structural properties of actinobacterial terminal oxidases

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