SwePub
Sök i LIBRIS databas

  Utökad sökning

WFRF:(Hederstedt Lars)
 

Sökning: WFRF:(Hederstedt Lars) > Role of His residue...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003283naa a2200313 4500
001oai:lup.lub.lu.se:c1c30663-a5cd-437e-8175-fcb811a8e741
003SwePub
008170718s1990 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/c1c30663-a5cd-437e-8175-fcb811a8e7412 URI
024a https://doi.org/10.1111/j.1365-2958.1990.tb00677.x2 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Fridén, Hu Lund University4 aut
2451 0a Role of His residues in Bacillus subtilis cytochrome b558 for haem binding and assembly of succinate:quinone oxidoreductase (complex II)
264 1b Wiley,c 1990
520 a Cytochrome 5558 in the cytoplasmic membrane ofBacilius subtiiis constitutes the anchor and electronacceptor to the flavoprotein (Fp) and iron-sulphurprotein (Ip) in succinate:quinone oxidoreductase, andseemingly contains two haem groups. EPR and MCDspectroscopic data indicate bis-imidazole ligation ofthe haem. Apo-cytochrome was found in the mem-brane fraction of haem-deficient B. subtilis, suggest-ing that during biogenesis of the oxidoreductase thecytochrome b558 polypeptide is embedded into themembrane prior to the incorporation of haem andsubsequent binding of Fp and Ip. The six His residuesin cytochrome b558 were individually changed to Tyrto attempt identification of residues serving as haemaxial ligands and to analyse the role of His residues forassembly and function of the oxidoreductase. Fromthe properties of the mutants, His-47 can be excludedas a haem ligand. The remaining His residues (atpositions 13,28,70,113 and 155) are located in or closeto four predicted transmembrane segments. TheTyr-28 and Tyr-70 mutant proteins appeared to lackone of the two haems. Only the Tyr-13 and Tyr-47mutant cytochromes were found to function asanchors for Fp and Ip, but the Tyr-13 mutant cyto-chrome assembles into an enzymatically defectivesuccinate:quinone oxidoreductase. It is concludedfrom a combination of the experimental findings,sequence comparisons and membrane topology datathat His-28, His-70 and His-155 are probably haemaxial ligands in a dihaem cytochrome 6558. His-70 andHis-155 may be tigands to the same haem.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
650 7a NATURVETENSKAPx Biologix Mikrobiologi0 (SwePub)106062 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Microbiology0 (SwePub)106062 hsv//eng
700a Hederstedt, Larsu Lund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science4 aut0 (Swepub:lu)mikb-lhe
710a Lund Universityb Molekylär cellbiologi4 org
773t Molecular Microbiologyd : Wileyg 4:6, s. 1045-1056q 4:6<1045-1056x 1365-2958x 0950-382X
856u http://dx.doi.org/10.1111/j.1365-2958.1990.tb00677.xy FULLTEXT
8564 8u https://lup.lub.lu.se/record/c1c30663-a5cd-437e-8175-fcb811a8e741
8564 8u https://doi.org/10.1111/j.1365-2958.1990.tb00677.x

Hitta via bibliotek

Till lärosätets databas

Hitta mer i SwePub

Av författaren/redakt...
Fridén, H
Hederstedt, Lars
Om ämnet
NATURVETENSKAP
NATURVETENSKAP
och Biologi
och Biokemi och mole ...
NATURVETENSKAP
NATURVETENSKAP
och Biologi
och Mikrobiologi
Artiklar i publikationen
Molecular Microb ...
Av lärosätet
Lunds universitet

Sök utanför SwePub

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy