Cyanide-insensitive quinol oxidase (CIO) from Gluconobacter oxydans is a unique terminal oxidase subfamily of cytochrome bd

Miura, Hiroshi; Mogi, Tatsushi; Ano, Yoshitaka; Migita, Catharina T.; Matsutani, Minenosuke; Yakushi, Toshiharu; Kita, Kiyoshi; Matsushita, Kazunobu

doi:10.1093/jb/mvt019

Cited by 36 publications

(25 citation statements)

References 56 publications

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“…The amino acid sequences of the two subunits of CIO, CioA and CioB, are highly similar to those of the canonical bd oxidases CydA and CydB, respectively, but the conserved sequence of the periplasmic loop (Q loop) that contains the putative quinol-oxidizing site is significantly shorter in CioA than in CydA (9). CIO of P. aeruginosa was predicted to have high affinity for oxygen, but its K m value for oxygen determined in this study was comparable to those of aa 3 and Cyo, indicating that it is a low-affinity enzyme, similar to the CIOs of C. jejuni and G. oxydans (Table 2) (13,14). The low affinity of CIOs for oxygen is in contrast to the high affinity of the canonical bd oxidase of E. coli (42,43).…”

Section: Figmentioning

confidence: 76%

“…1B) clearly showed that P. aeruginosa CIO is a low-affinity enzyme, similar to the CIOs of C. jejuni and G. oxydans (13,14). The low affinity of these CIOs is in contrast to the high affinity of the canonical bd oxidase of E. coli (42).…”

Section: Five Terminal Oxidases Of P Aeruginosamentioning

confidence: 98%

“…The copper-free quinol oxidase CIO belongs to the cytochrome bd family but is phylogenetically and characteristically distinct from the canonical bd oxidases (9)(10)(11)(12)(13)(14). The amino acid sequences of the two subunits of CIO, CioA and CioB, are highly similar to those of the canonical bd oxidases CydA and CydB, respectively, but the conserved sequence of the periplasmic loop (Q loop) that contains the putative quinol-oxidizing site is significantly shorter in CioA than in CydA (9).…”

Section: Figmentioning

confidence: 99%

“…CIO belongs to the cytochrome bd family, and although its primary structure is similar to those of canonical bd oxidases, it is phylogenetically distinct (9)(10)(11). Recent analyses in Gluconobacter oxydans showed that the CIO contains hemes b 558 , b 595 , and d, as in the case of canonical bd oxidases, and has a high turnover rate (12,13). The cytochrome bd oxidase of E. coli has high affinity for oxygen, whereas CIOs of Campylobacter jejuni and G. oxydans have low affinity for oxygen (13,14).…”

mentioning

confidence: 99%

“…Recent analyses in Gluconobacter oxydans showed that the CIO contains hemes b 558 , b 595 , and d, as in the case of canonical bd oxidases, and has a high turnover rate (12,13). The cytochrome bd oxidase of E. coli has high affinity for oxygen, whereas CIOs of Campylobacter jejuni and G. oxydans have low affinity for oxygen (13,14). In contrast, the CIO of P. aeruginosa was predicted to have high affinity for oxygen because a cco1 cco2 double mutant, which lacked cbb 3 -1 and cbb 3 -2, was able to grow under microaerobic conditions (2% O 2 ), but a cco1 cco2 cio triple mutant, which lacked cbb 3 -1, cbb 3 -2, and CIO, did not grow under such conditions (15).…”

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confidence: 99%

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Enzymatic Characterization and In Vivo Function of Five Terminal Oxidases in Pseudomonas aeruginosa

et al. 2014

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The ubiquitous opportunistic pathogen Pseudomonas aeruginosa has five aerobic terminal oxidases: bo 3 -type quinol oxidase (Cyo), cyanide-insensitive oxidase (CIO), aa 3 -type cytochrome c oxidase (aa 3 ), and two cbb 3 -type cytochrome c oxidases (cbb 3 -1 and cbb 3 -2). These terminal oxidases are differentially regulated under various growth conditions and are thought to contribute to the survival of this microorganism in a wide variety of environmental niches. Here, we constructed multiple mutant strains of P. aeruginosa that express only one aerobic terminal oxidase to investigate the enzymatic characteristics and in vivo function of each enzyme. The K m values of Cyo, CIO, and aa 3 for oxygen were similar and were 1 order of magnitude higher than those of cbb 3 -1 and cbb 3 -2, indicating that Cyo, CIO, and aa 3 are low-affinity enzymes and that cbb 3 -1 and cbb 3 -2 are high-affinity enzymes. Although cbb 3 -1 and cbb 3 -2 exhibited different expression patterns in response to oxygen concentration, they had similar K m values for oxygen. Both cbb 3 -1 and cbb 3 -2 utilized cytochrome c 4 as the main electron donor under normal growth conditions. The electron transport chains terminated by cbb 3 -1 and cbb 3 -2 generate a proton gradient across the cell membrane with similar efficiencies. The electron transport chain of aa 3 had the highest proton translocation efficiency, whereas that of CIO had the lowest efficiency. The enzymatic properties of the terminal oxidases reported here are partially in agreement with their regulatory patterns and may explain the environmental adaptability and versatility of P. aeruginosa.

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Section: Figmentioning

confidence: 76%

Section: Five Terminal Oxidases Of P Aeruginosamentioning

confidence: 98%

Section: Figmentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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Enzymatic Characterization and In Vivo Function of Five Terminal Oxidases in Pseudomonas aeruginosa

et al. 2014

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Unique glucose oxidation catalysis of Gluconobacter oxydans constitutes an efficient cellulosic gluconic acid fermentation free of inhibitory compounds disturbance

Zhou

Yao

Zhang

et al. 2019

Biotech & Bioengineering

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Toxic inhibitory compounds from lignocellulose pretreatment are the major obstacle to achieve high bioconversion efficiency in biorefinery fermentations. This study shows a unique glucose oxidation catalysis of Gluconobacter oxydans with its gluconic acid productivity free of inhibitor disturbance. The microbial experimentations and the transcriptome analysis revealed that both the activity of the membrane-bound glucose dehydrogenase and the transcription level of the genes in periplasmic glucose oxidation respiratory chain of G. oxydans were essentially not affected in the presence of inhibitory compounds. G. oxydans also rapidly converted furan and phenolic aldehyde inhibitors into the less toxic alcohols or acids. The synergy of the robust periplasmic glucose oxidation and the rapid inhibitor conversion of G. oxydans significantly elevated the efficiency of the oxidative fermentation in lignocellulose hydrolysate. The corresponding genes responsible for the conversion of furan and phenolic aldehyde inhibitors were also mined by DNA microarrays. The synergistic mechanism of G. oxydans provided an important option of metabolic modification for enhancing inhibitor tolerance of general fermentation strains. K E Y W O R D S gluconobacter oxydans, inhibitor tolerance, lignocellulose, membrane-bound glucose dehydrogenase (mGDH), oxidative fermentation

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The Family Acetobacteraceae

Komagata¹,

Iino²,

Yamada³

2014

The Prokaryotes

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Cyanide-insensitive quinol oxidase (CIO) from Gluconobacter oxydans is a unique terminal oxidase subfamily of cytochrome bd

Cited by 36 publications

References 56 publications

Enzymatic Characterization and In Vivo Function of Five Terminal Oxidases in Pseudomonas aeruginosa

Enzymatic Characterization and In Vivo Function of Five Terminal Oxidases in Pseudomonas aeruginosa

Unique glucose oxidation catalysis of Gluconobacter oxydans constitutes an efficient cellulosic gluconic acid fermentation free of inhibitory compounds disturbance

The Family Acetobacteraceae

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