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Poole’s laboratory was the first to identify correctly the nature of spectrally distinct forms of the alternative E. coli oxidase (cytochrome bd). He also showed the unique functional capabilities of this oxidase, including its remarkably high affinity for oxygen and its role in protecting E. coli from nitric oxide.
In the aerobic diazotroph Azotobacter vinelandii, his group demonstrated the critical role of this oxidase in aerotolerant nitrogen fixation in the process known as respiratory protection. This advanced our understanding of the cytochrome bd-type oxidase by demonstrating that its assembly requires a membrane transport complex, CydDC, the first bacterial example of a heterodimeric ABC (ATP-Binding Cassette) transporter homologous to the cystic fibrosis chloride channel (CFTR).
He subsequently demonstrated that it exports cysteine and glutathione to the bacterial periplasm and its importance for maintaining the redox environment required for cytochrome assembly in the periplasm.
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Advances in Microbial Physiology (2023): IX-IX
Veterinary Microbiology (2023): 109819-109819
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Veterinary microbiology (2023): 109819
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