Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Danielle Lemesle-Meunier"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1555:37-43
Acidithiobacillus ferrooxidans is an acidophilic chemolithotrophic bacterium that can grow in the presence of either a weak reductant, Fe(2+), or reducing sulfur compounds that provide more energy for growth than Fe(2+). Here we first review the late
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::805ff62fd10fbade9eefcc798bd6c89e
https://doi.org/10.1016/s0005-2728(02)00251-7
https://doi.org/10.1016/s0005-2728(02)00251-7
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1506:89-102
Four totally conserved glycines are involved in the packing of the two cytochrome b hemes, b(L) and b(H), of the bc(1) complex. The conserved glycine 131 is involved in the packing of heme b(L) and is separated by only 3 A from this heme in the bc(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f877e0f69668690234203fb4ba9b4b53
https://doi.org/10.1016/s0005-2728(01)00186-4
https://doi.org/10.1016/s0005-2728(01)00186-4
Publikováno v:
Journal of Bacteriology. 182:3602-3606
The energy-dependent electron transfer pathway involved in the reduction of pyridine nucleotides which is required for CO 2 fixation to occur in the acidophilic chemolithotrophic organism Thiobacillus ferrooxidans was investigated using ferrocytochro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fb6c02387e3c7fadde75c454eb7d970a
https://doi.org/10.1128/jb.182.12.3602-3606.2000
https://doi.org/10.1128/jb.182.12.3602-3606.2000
Autor:
Wolfgang Nitschke, Bruno Guigliarelli, Myriam Brugna, Marcel Asso, Christian L. Schmidt, Danielle Lemesle-Meunier
Publikováno v:
Journal of Biological Chemistry. 274:16766-16772
The Rieske proteins of two phylogenetically distant acidophilic organisms, i.e. the proteobacteriumThiobacillus ferrooxidans and the crenarchaeonSulfolobus acidocaldarius, were studied by EPR. Redox titrations at a range of pH values showed that the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d0186ceec6ac6b0b9d12d8ac093d56e
https://doi.org/10.1074/jbc.274.24.16766
https://doi.org/10.1074/jbc.274.24.16766
Publikováno v:
Journal of Biological Chemistry. 274:16760-16765
The redox components of the cytochromebc 1 complex from the acidophilic chemolithotrophic organism Thiobacillus ferrooxidans were investigated by potentiometric and spectroscopic techniques. Optical redox titrations demonstrated the presence of two b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d891f3125850738a6d7d542be015b031
https://doi.org/10.1074/jbc.274.24.16760
https://doi.org/10.1074/jbc.274.24.16760
Autor:
Richard A. Rothery, Francis Blasco, Axel Magalon, Joel H. Weiner, Chantal Frixon, Danielle Lemesle-Meunier
Publikováno v:
Journal of Biological Chemistry. 273:10851-10856
We have used inhibitors and site-directed mutants to investigate quinol binding to the cytochromeb nr (NarI) of Escherichia colinitrate reductase (NarGHI). Both stigmatellin and 2-n-heptyl-4-hydroxyquinoline-N-oxide (HOQNO) inhibit menadiol:nitrate o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d886f7b5f037957c0b96d016b021ed07
https://doi.org/10.1074/jbc.273.18.10851
https://doi.org/10.1074/jbc.273.18.10851
Autor:
Francis Blasco, Richard A. Rothery, Danielle Lemesle-Meunier, Joel H. Weiner, Axel Magalon, Chantal Frixon
Publikováno v:
Journal of Biological Chemistry. 272:25652-25658
Optical spectroscopy and EPR studies confirm the existence of two b-type hemes in the NarI subunit (cytochrome b nr) of the membrane-bound nitrate reductase (NarGHI) of Escherichia coli. Replacement of His-56 by Arg and His-66 by Tyr results in the l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4ef7e47fabb0488a0e11a8f9808ceb1
https://doi.org/10.1074/jbc.272.41.25652
https://doi.org/10.1074/jbc.272.41.25652
Autor:
Piotr P. Slonimski, Paule Brivet-Chevillotte, Christophe Bruel, N Forget, Danielle Lemesle-Meunier, J P di Rago, T Tron
Publikováno v:
Journal of Biological Chemistry. 268:15626-15632
We characterized six novel missense mutations in mitochondrial cytochrome b (C133Y, W142R, S206L, M221K, L282F, and G340E) which impair the respiratory growth of yeast and which have differential effects on the functioning and assembly of the bc1 com
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3a82e2bd3b00406c2b413724845736ec
https://doi.org/10.1016/s0021-9258(18)82302-x
https://doi.org/10.1016/s0021-9258(18)82302-x
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2008, 47 (8), pp.2357-68. ⟨10.1021/bi701905a⟩
Biochemistry, American Chemical Society, 2008, 47 (8), pp.2357-68. ⟨10.1021/bi701905a⟩
International audience; The mitochondrial bc1 complex catalyzes the oxidation of ubiquinol and the reduction of cytochrome (cyt) c coupled to a vectorial translocation of protons across the membrane. On the basis of the three-dimensional structures o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34629deb75498151696b4962066da665
https://hal.archives-ouvertes.fr/hal-00473793
https://hal.archives-ouvertes.fr/hal-00473793
Autor:
Thierry Tron, Danielle Lemesle-Meunier
Publikováno v:
Current Genetics. 18:413-419
Two cytochrome b respiratory-deficient mutants were sequenced and their DNA base change identified, leading to the replacement of glycine (G137 by valine or glutamic acid. No variation in their cytochrome b content with regard to cytochrome oxidase a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc669fdeecb36f75ae6c8e9df2896a54
https://doi.org/10.1007/bf00309910
https://doi.org/10.1007/bf00309910