Zobrazeno 1 - 10
of 472
pro vyhledávání: '"Heme B"'
Akademický článek
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Publikováno v:
Molecules, Vol 28, Iss 8, p 3633 (2023)
Heme b, which is characterized by a ferrous ion and a porphyrin macrocycle, acts as a prosthetic group for many enzymes and contributes to various physiological processes. Consequently, it has wide applications in medicine, food, chemical production,
Externí odkaz:
https://doaj.org/article/e8a86a1fc1c842828560d78dfb2a389c
Autor:
Evangelia Louropoulou, Martha Gledhill, Thomas J. Browning, Dhwani K. Desai, Jan-Lukas Menzel Barraqueta, Manon Tonnard, Géraldine Sarthou, Hélène Planquette, Andrew R. Bowie, Ruth A. Schmitz, Julie LaRoche, Eric P. Achterberg
Publikováno v:
Frontiers in Microbiology, Vol 10 (2019)
Heme b is an iron-containing co-factor in hemoproteins. Heme b concentrations are low (0.7 μm) from the North Atlantic Ocean (GEOVIDE cruise – GEOTRACES section GA01), which spanned several biogeochemical regimes. We examined the relationship betw
Externí odkaz:
https://doaj.org/article/6fafc95d328248a6843522f58d5237a8
Publikováno v:
Critical Reviews in Biochemistry and Molecular Biology. 56:640-668
Aerobic respiration is a key energy-producing pathway in many prokaryotes and virtually all eukaryotes. The final step of aerobic respiration is most commonly catalyzed by heme-copper oxidases embedded in the cytoplasmic or mitochondrial membrane. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e7cafd11bd396979409a0aba9bdb9eb2
https://doi.org/10.1080/10409238.2021.1957668
https://doi.org/10.1080/10409238.2021.1957668
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
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Autor:
Hongbo Huang, Changbiao Chi, Xiaoqi Ji, Ming Ma, Jiajia Tu, Wenjuan Ding, Qinglian Li, Jianhua Ju, Ziwei Yao
Publikováno v:
ACS Omega, Vol 5, Iss 32, Pp 20548-20557 (2020)
ACS Omega
ACS Omega
Diels–Alder (DA) [4 + 2]-cycloaddition reactions rank among the most powerful transformations in synthetic organic chemistry; biosynthetic examples, however, are few and far between. We report here a heme-binding cyclase, AbmU, that catalyzes an es
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d387b27da9da14fc745f569361781b60
https://doaj.org/article/bc54b58c5c15427593303d9cbf6cf7ca
https://doaj.org/article/bc54b58c5c15427593303d9cbf6cf7ca
Autor:
Andrew P. Hunt, Matthew R. Dent, Nicolai Lehnert, Michael W. Milbauer, Subhra Samanta, Judith N. Burstyn
Publikováno v:
Inorganic Chemistry. 59:8034-8043
Cytochrome (Cyt) P450s are an important class of enzymes with numerous functions in nature. The unique reactivity of these enzymes relates to their heme b active sites with an axially bound, deprot...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4e98e6e6ce99e4b9a818fee55a659d7
https://doi.org/10.1021/acs.inorgchem.0c00245
https://doi.org/10.1021/acs.inorgchem.0c00245
Autor:
Daniela Cioloboc, Silvano R. Valandro, Kirk S. Schanze, Donald M. Kurtz, Alexander B. Taylor, Brenda S. Benavides
Publikováno v:
Biochemistry
The iron storage protein bacterioferritin (Bfr) binds up to 12 hemes b at specific sites in its protein shell. The heme b can be substituted with the photosensitizer Zn(II)-protoporphyrin IX (ZnPP), and photosensitized reductive iron release from the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ce1bdbb4ea3d7918132997fcdb6372d
https://doi.org/10.1021/acs.biochem.9b01103
https://doi.org/10.1021/acs.biochem.9b01103
Autor:
Kristina Djinović-Carugo, Stefan Hofbauer, Christian Obinger, Bettina Lier, Paul G. Furtmüller, Vera Pfanzagl, Chris Oostenbrink, Hanna Michlits
Publikováno v:
ACS Catalysis
Coproheme decarboxylases (ChdCs) catalyze the final step in heme b biosynthesis of monoderm and some diderm bacteria. In this reaction, coproheme is converted to heme b via monovinyl monopropionate deuteroheme (MMD) in two consecutive decarboxylation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99703bb7c5f29da94288a765c8118bba
https://doi.org/10.1021/acscatal.0c00411
https://doi.org/10.1021/acscatal.0c00411
Autor:
Mathias O. Senge, Elisabeth Sitte
Publikováno v:
European Journal of Organic Chemistry
Protoporphyrin IX (PPIX) is the porphyrin scaffold of heme b, a ubiquitous prosthetic group of proteins responsible for oxygen binding (hemoglobin, myoglobin), electron transfer (cytochrome c) and catalysis (cytochrome P450, catalases, peroxidases).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff8ba3d813be21bd400268034adcff53
https://doi.org/10.1002/ejoc.202000074
https://doi.org/10.1002/ejoc.202000074