Occurrence and sequence of Sphaeroides Heme Protein and Diheme Cytochrome C in purple photosynthetic bacteria in the family Rhodobacteraceae

Persistent Link:
http://hdl.handle.net/10150/610087
Title:
Occurrence and sequence of Sphaeroides Heme Protein and Diheme Cytochrome C in purple photosynthetic bacteria in the family Rhodobacteraceae
Author:
Meyer, Terry; Kyndt, John; Cusanovich, Michael
Affiliation:
Department of Chemistry and Biochemistry, University of Arizona, Tucson Arizona 85721 USA
Issue Date:
2010
Publisher:
BioMed Central
Citation:
Meyer et al. BMC Biochemistry 2010, 11:24 http://www.biomedcentral.com/1471-2091/11/24
Journal:
BMC Biochemistry
Rights:
© 2010 Meyer et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0)
Collection Information:
This item is part of the UA Faculty Publications collection. For more information this item or other items in the UA Campus Repository, contact the University of Arizona Libraries at repository@u.library.arizona.edu.
Abstract:
BACKGROUND:Sphaeroides Heme Protein (SHP) was discovered in the purple photosynthetic bacterium, Rhodobacter sphaeroides, and is the only known c-type heme protein that binds oxygen. Although initially not believed to be widespread among the photosynthetic bacteria, the gene has now been found in more than 40 species of proteobacteria and generally appears to be regulated. Rb. sphaeroides is exceptional in not having regulatory genes associated with the operon. We have thus analyzed additional purple bacteria for the SHP gene and examined the genetic context to obtain new insights into the operon, its distribution, and possible function.RESULTS:We found SHP in 9 out of 10 strains of Rb. sphaeroides and in 5 out of 10 purple photosynthetic bacterial species in the family Rhodobacteraceae. We found a remarkable similarity within the family including the lack of regulatory genes. Within the proteobacteria as a whole, SHP is part of a 3-6 gene operon that includes a membrane-spanning diheme cytochrome b and one or two diheme cytochromes c. Other genes in the operon include one of three distinct sensor kinase - response regulators, depending on species, that are likely to regulate SHP.CONCLUSIONS:SHP is not as rare as generally believed and has a role to play in the photosynthetic bacteria. Furthermore, the two companion cytochromes along with SHP are likely to function as an electron transfer pathway that results in the reduction of SHP by quinol and formation of the oxygen complex, which may function as an oxygenase. The three distinct sensors suggest at least as many separate functional roles for SHP. Two of the sensors are not well characterized, but the third is homologous to the QseC quorum sensor, which is present in a number of pathogens and typically appears to regulate genes involved in virulence.
EISSN:
1471-2091
DOI:
10.1186/1471-2091-11-24
Version:
Final published version
Additional Links:
http://www.biomedcentral.com/1471-2091/11/24

Full metadata record

DC FieldValue Language
dc.contributor.authorMeyer, Terryen
dc.contributor.authorKyndt, Johnen
dc.contributor.authorCusanovich, Michaelen
dc.date.accessioned2016-05-20T08:58:16Z-
dc.date.available2016-05-20T08:58:16Z-
dc.date.issued2010en
dc.identifier.citationMeyer et al. BMC Biochemistry 2010, 11:24 http://www.biomedcentral.com/1471-2091/11/24en
dc.identifier.doi10.1186/1471-2091-11-24en
dc.identifier.urihttp://hdl.handle.net/10150/610087-
dc.description.abstractBACKGROUND:Sphaeroides Heme Protein (SHP) was discovered in the purple photosynthetic bacterium, Rhodobacter sphaeroides, and is the only known c-type heme protein that binds oxygen. Although initially not believed to be widespread among the photosynthetic bacteria, the gene has now been found in more than 40 species of proteobacteria and generally appears to be regulated. Rb. sphaeroides is exceptional in not having regulatory genes associated with the operon. We have thus analyzed additional purple bacteria for the SHP gene and examined the genetic context to obtain new insights into the operon, its distribution, and possible function.RESULTS:We found SHP in 9 out of 10 strains of Rb. sphaeroides and in 5 out of 10 purple photosynthetic bacterial species in the family Rhodobacteraceae. We found a remarkable similarity within the family including the lack of regulatory genes. Within the proteobacteria as a whole, SHP is part of a 3-6 gene operon that includes a membrane-spanning diheme cytochrome b and one or two diheme cytochromes c. Other genes in the operon include one of three distinct sensor kinase - response regulators, depending on species, that are likely to regulate SHP.CONCLUSIONS:SHP is not as rare as generally believed and has a role to play in the photosynthetic bacteria. Furthermore, the two companion cytochromes along with SHP are likely to function as an electron transfer pathway that results in the reduction of SHP by quinol and formation of the oxygen complex, which may function as an oxygenase. The three distinct sensors suggest at least as many separate functional roles for SHP. Two of the sensors are not well characterized, but the third is homologous to the QseC quorum sensor, which is present in a number of pathogens and typically appears to regulate genes involved in virulence.en
dc.language.isoenen
dc.publisherBioMed Centralen
dc.relation.urlhttp://www.biomedcentral.com/1471-2091/11/24en
dc.rights© 2010 Meyer et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0)en
dc.titleOccurrence and sequence of Sphaeroides Heme Protein and Diheme Cytochrome C in purple photosynthetic bacteria in the family Rhodobacteraceaeen
dc.typeArticleen
dc.identifier.eissn1471-2091en
dc.contributor.departmentDepartment of Chemistry and Biochemistry, University of Arizona, Tucson Arizona 85721 USAen
dc.identifier.journalBMC Biochemistryen
dc.description.collectioninformationThis item is part of the UA Faculty Publications collection. For more information this item or other items in the UA Campus Repository, contact the University of Arizona Libraries at repository@u.library.arizona.edu.en
dc.eprint.versionFinal published versionen
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