| pubmed-article:20955518 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20955518 | lifeskim:mentions | umls-concept:C0080118 | lld:lifeskim |
| pubmed-article:20955518 | lifeskim:mentions | umls-concept:C0456603 | lld:lifeskim |
| pubmed-article:20955518 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:20955518 | lifeskim:mentions | umls-concept:C0253830 | lld:lifeskim |
| pubmed-article:20955518 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:20955518 | pubmed:dateCreated | 2010-10-27 | lld:pubmed |
| pubmed-article:20955518 | pubmed:abstractText | Substrate channeling between the enzymatic steps in the (bacterio)chlorophyll biosynthetic pathway catalyzed by magnesium chelatase (BchI/ChlI, BchD/ChlD and BchH/ChlH subunits) and S-adenosyl-L-methionine:magnesium-protoporphyrin IX O-methyltransferase (BchM/ChlM) has been suggested. This involves delivery of magnesium-protoporphyrin IX from the BchH/ChlH subunit of magnesium chelatase to BchM/ChlM. Stimulation of BchM/ChlM activity by BchH/ChlH has previously been shown, and physical interaction of the two proteins has been demonstrated. In plants and cyanobacteria, there is an added layer of complexity, as Gun4 serves as a porphyrin (protoporphyrin IX and magnesium-protoporphyrin IX) carrier, but this protein does not exist in anoxygenic photosynthetic bacteria. BchJ may play a similar role to Gun4 in Rhodobacter, as it has no currently assigned function in the established pathway. Purified recombinant Rhodobacter capsulatus BchJ and BchM were found to cause a shift in the equilibrium amount of Mg-protoporphyrin IX formed in a magnesium chelatase assay. Analysis of this shift revealed that it was always in a 1 : 1 ratio with either of these proteins and the BchH subunit of the magnesium chelatase. The establishment of the new equilibrium was faster with BchM than with BchJ in a coupled magnesium chelatase assay. BchJ bound magnesium-protoporphyrin IX or formed a ternary complex with BchH and magnesium-protoporphyrin IX. These results suggest that BchJ may play a role as a general magnesium porphyrin carrier, similar to one of the roles of GUN4 in oxygenic organisms. | lld:pubmed |
| pubmed-article:20955518 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20955518 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20955518 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20955518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20955518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20955518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20955518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20955518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20955518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20955518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20955518 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20955518 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:20955518 | pubmed:issn | 1742-4658 | lld:pubmed |
| pubmed-article:20955518 | pubmed:author | pubmed-author:WillowsRobert... | lld:pubmed |
| pubmed-article:20955518 | pubmed:author | pubmed-author:SawickiArturA | lld:pubmed |
| pubmed-article:20955518 | pubmed:copyrightInfo | © 2010 The Authors Journal compilation © 2010 FEBS. | lld:pubmed |
| pubmed-article:20955518 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20955518 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:20955518 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20955518 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20955518 | pubmed:pagination | 4709-21 | lld:pubmed |
| pubmed-article:20955518 | pubmed:meshHeading | pubmed-meshheading:20955518... | lld:pubmed |
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| pubmed-article:20955518 | pubmed:meshHeading | pubmed-meshheading:20955518... | lld:pubmed |
| pubmed-article:20955518 | pubmed:meshHeading | pubmed-meshheading:20955518... | lld:pubmed |
| pubmed-article:20955518 | pubmed:meshHeading | pubmed-meshheading:20955518... | lld:pubmed |
| pubmed-article:20955518 | pubmed:meshHeading | pubmed-meshheading:20955518... | lld:pubmed |
| pubmed-article:20955518 | pubmed:meshHeading | pubmed-meshheading:20955518... | lld:pubmed |
| pubmed-article:20955518 | pubmed:meshHeading | pubmed-meshheading:20955518... | lld:pubmed |
| pubmed-article:20955518 | pubmed:meshHeading | pubmed-meshheading:20955518... | lld:pubmed |
| pubmed-article:20955518 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20955518 | pubmed:articleTitle | BchJ and BchM interact in a 1 : 1 ratio with the magnesium chelatase BchH subunit of Rhodobacter capsulatus. | lld:pubmed |
| pubmed-article:20955518 | pubmed:affiliation | Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney, NSW, Australia. | lld:pubmed |
| pubmed-article:20955518 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20955518 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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