Escherichia coli MG1655 cells expressing novel bacterial hemoglobin and flavohemoglobin
genes from a medium-copy-number plasmid were grown in shake flask cultures under …

Hemoglobin homologs are being identified in an expanding number of unicellular
prokaryotic and eukaryotic organisms. Many of these hemoglobins are twodomain proteins …

Escherichia coli possesses a flavohemoglobin (Hmp), product of hmp, the first microbial
globin gene to be sequenced and characterized at the molecular level. Although related …

Escherichia coli possesses a two-domain flavohemoglobin, Hmp, implicated in nitric oxide
(NO) detoxification. To determine the contribution of each domain of Hmp toward NO …

Escherichia coli possesses a soluble flavohemoglobin, with an unknown function, encoded
by the hmp gene. A monolysogen containing an hmp-lacZ operon fusion was constructed to …

Nitric-oxide dioxygenase (NOD) and reductase (NOR) activities of flavohemoglobin
(flavoHb) have been suggested as mechanisms for NO metabolism and detoxification in a …

Nitric oxide (NO•) is a toxin, and various life forms appear to have evolved strategies for its
detoxification. NO•-resistant mutants of Escherichia coli were isolated that rapidly consumed …

Yeast hemoglobin was discovered close to half a century ago, but its function has remained
unknown. Herein, we report that this flavohemoglobin protects Saccharomyces cerevisiae …

Respiration of Escherichia colicatalyzed either by cytochrome bo′ or bd is sensitive to
micromolar extracellular NO; extensive, transient inhibition of respiration increases as …

Campylobacter jejuni expresses two hemoglobins, each of which exhibits a heme pocket
and structural signatures in common with vertebrate and plant globins. One of these …