Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity.

  title={Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity.},
  author={B. Li and J. Anderson and C. Mowat and C. Miles and G. Reid and S. Chapman},
  journal={Biochemical Society transactions},
  volume={36 Pt 5},
Rhodobacter sphaeroides produces a novel cytochrome, designated as SHP (sphaeroides haem protein), that is unusual in having asparagine as a redox-labile haem ligand. The gene encoding SHP is contained within an operon that also encodes a DHC (dihaem cytochrome c) and a membrane-associated cytochrome b. DHC and SHP have been shown to have high affinity for each other at low ionic strength (Kd=0.2 microM), and DHC is able to reduce SHP very rapidly. The reduced form of the protein, SHP2… Expand
Functional studies on a novel cytochrome c from Rhodobacter sphaeroides
ii ABSTRACT SHP (Sphaeroides Heme Protein) is a monoheme cytochrome c of unknown function. In general, ligands cannot bind to ferric SHP, but some diatomic molecules, such as O2 or NO, can bind toExpand
Occurrence and sequence of Sphaeroides Heme Protein and Diheme Cytochrome C in purple photosynthetic bacteria in the family Rhodobacteraceae
SHP is not as rare as generally believed and has a role to play in the photosynthetic bacteria and the three distinct sensors suggest at least as many separate functional roles for SHP. Expand
Hemoglobin: A Nitric-Oxide Dioxygenase
NOD knockout organisms and cells expressing recombinant NODs are helping to advance the understanding of NO actions in microbial infection, plant senescence, cancer, mitochondrial function, iron metabolism, and tissue O2 homeostasis. Expand
Cytochromes c': Structure, Reactivity and Relevance to Haem-Based Gas Sensing.
How structural features of cytochromes c' influence haem spectroscopy and reactivity with NO, CO and O2 and the relevance of cy tochrome c' to understanding the mechanisms of gas binding to haem-based sensor proteins is discussed. Expand
The impact of nitrite on aerobic growth of Paracoccus denitrificans PD1222
The effect of nitrite stress induced in Paracoccus denitrificans PD1222 was examined using additions of sodium nitrite to an aerobic bacterial culture. Nitrite generates a strong stress response inExpand
Phosphate limitation increases coenzyme Q10 production in industrial Rhodobacter sphaeroides HY01
Results indicated that phosphate limitation combined with glucose fed-batch fermentation represented an effective strategy for CoQ10 production in the HY01, and that improved CoQ 10 biosynthesis efficiency was possibly related to the disturbance of energy metabolism and redox potential. Expand


Crystal Structures of an Oxygen-binding Cytochrome cfrom Rhodobacter sphaeroides *
The photosynthetic bacterium Rhodobacter sphaeroides produces a heme protein (SHP), which is an unusual c-type cytochrome capable of transiently binding oxygen during autooxidation, and the three-dimensional structure represents a new variation of the class I cy tochrome c fold. Expand
Structural and functional studies on DHC, the diheme cytochrome c from Rhodobacter sphaeroides, and its interaction with SHP, the sphaeroides heme protein.
Structural-function studies on the diheme cytochrome c have carried out and its interaction with SHP is examined, showing that DHC binds strongly to its proposed physiological partner, SHP, and is very efficient in electron transfer to SHP. Expand
Soluble cytochrome composition of the purple phototrophic bacterium, Rhodopseudomonas sphaeroides ATCC 17023.
A detailed study of the soluble cytochrome composition of Rhodopseudomonas sphaeroides indicates that there are five c-type cytochromes and one b-type Cytochrome present, and an unusual high-spin c- type heme protein has been isolated. Expand
Cytochrome c" from the obligate methylotroph Methylophilus methylotrophus, an unexpected homolog of sphaeroides heme protein from the phototroph Rhodobacter sphaeroides.
The complete primary structure of an unusual soluble cytochrome c isolated from the obligate methylotrophic bacterium Methylophilus methylotrophus has been determined to contain 124 amino acids andExpand
The Flavohemoglobin of Escherichia coli Confers Resistance to a Nitrosating Agent, a “Nitric Oxide Releaser,” and Paraquat and Is Essential for Transcriptional Responses to Oxidative Stress*
It is concluded that Hmp plays a role in protection from nitrosating agents and NO-related species and oxidative stress, which probably involves direct detoxification of those species and sensing of NO- related and oxidative Stress. Expand
Nitric-oxide Dioxygenase Activity and Function of Flavohemoglobins
The results suggest that flavoHbs and related hemoglobins evolved as NO detoxifying components of nitrogen metabolism capable of discriminating O2 from inhibitory NO and CO. Expand
Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases.
  • P. R. Gardner
  • Chemistry, Medicine
  • Journal of inorganic biochemistry
  • 2005
High affinity flavoHb and Hb heme ligands, and other inhibitors, may find application as antibiotics and antitumor agents that enhance the toxicity of immune cell-derived *NO or as vasorelaxants that increase *NO signalling. Expand
Ligand binding and covalent structure of an oxygen-binding heme protein from Rhodobacter sphaeroides, a representative of a new structural family of c-type cytochromes.
SHP is thus distantly related to small class I c-type cytochromes but is representative of a distinct family by virtue of its high-spin nature, the lack of a strong sixth ligand, and its capacity to bind oxygen. Expand
A NapC/NirT‐type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes
It is concluded that the electron transfer from menaquinol to the catalytic subunit (NrfA) of W. succinogenes nitrite reductase is mediated by NrfH, and the products of nrfI and nrfJ resemble proteins involved in cytochrome c biogenesis. Expand
Ligand binding properties of bacterial hemoglobins and flavohemoglobins.
Data suggest that differences exist between the mechanisms of ligand binding to bacterial hemoglobins and flavohemoglOBins, suggesting different functions in the cell. Expand