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	1.	The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition. [electronic resource] by D'mello, Rita Hill, Susan Poole, Robert K Producer: 19961231 In: Microbiology (Reading, England) vol. 142 ( Pt 4) Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	2.	Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: sensitivity of oxidoreductase activity to haem-bound dioxygen. [electronic resource] by Poole, Robert K Rogers, Nicola J D'mello, Rita A M Hughes, Martin N Orii, Yutaka Producer: 19970721 In: Microbiology (Reading, England) vol. 143 ( Pt 5) Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	3.	An unusual cytochrome o'-type cytochrome c oxidase in a Bacillus cereus cytochrome a3 mutant has a very high affinity for oxygen. [electronic resource] by Contreras, Martha L Escamilla, J Edgardo Del Arenal, I Patricia Dávila, J R D'mello, Rita Poole, Robert K Producer: 19991028 In: Microbiology (Reading, England) vol. 145 ( Pt 7) Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)

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