Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Biswash Thakuri"'
Autor:
Michael D. Roy, Michael J. Trenerry, Biswash Thakuri, Samantha N. MacMillan, Matthew D. Liptak, Kyle M. Lancaster, John F. Berry
Publikováno v:
Inorganic Chemistry. 61:3443-3457
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f550747bca0659d3b02efea66fc03c7
https://doi.org/10.1021/acs.inorgchem.1c03346
https://doi.org/10.1021/acs.inorgchem.1c03346
Publikováno v:
Biochemistry
The noncanonical heme oxygenase MhuD from Mycobacterium tuberculosis binds a heme substrate that adopts a dynamic equilibrium between planar and out-of-plane ruffled conformations. MhuD degrades this substrate to an unusual mycobilin product via succ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdd2bd5320ca0b580a6354b53f7d61fb
https://pubmed.ncbi.nlm.nih.gov/33729746
https://pubmed.ncbi.nlm.nih.gov/33729746
The non-canoncial heme oxygenase MhuD from Mycobacterium tuberculosis binds a heme substrate that adopts a dynamic equilibrium between planar and out-of-plane ruffled conformations. MhuD degrades this substrate to an unusual mycobilin product via suc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4e158bff5a3b63c894d04e1889eaaa6
https://doi.org/10.26434/chemrxiv.13171634.v4
https://doi.org/10.26434/chemrxiv.13171634.v4
The non-canoncial haem oxygenase MhuD from Mycobacterium tuberculosis binds a haem substrate that adopts a dynamic equilibrium between planar and out-of-plane ruffled conformations. MhuD degrades this substrate to an unusual mycobilin product via suc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::46f575b3ed6c07eb12ebfb787d3d56d0
https://doi.org/10.26434/chemrxiv.13171634.v1
https://doi.org/10.26434/chemrxiv.13171634.v1
Autor:
Sommer L Johansen, Amanda B. Graves, Matthew D. Liptak, Celia W. Goulding, Biswash Thakuri, Alex Chao
Publikováno v:
Metallomics : integrated biometal science, vol 10, iss 11
MhuD is a protein found in mycobacteria that can bind up to two heme molecules per protein monomer and catalyze the degradation of heme to mycobilin in vitro. Here the K(d1) for heme dissociation from heme-bound MhuD was determined to be 7.6 ± 0.8 n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35eb8e0b2b88293fe27010821dc3b96d
https://europepmc.org/articles/PMC6529808/
https://europepmc.org/articles/PMC6529808/
Publikováno v:
Metallomics; Nov2018, Vol. 10 Issue 11, p1543-1548, 6p
Autor:
Thakuri, Biswash, Graves, Amanda B., Chao, Alex, Johansen, Sommer L., Goulding, Celia W., Liptak, Matthew D.
Publikováno v:
Metallomics; Nov2018, Vol. 10 Issue 11, p1560-1563, 4p