Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Amanda B. Graves"'
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
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/
Crystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuD
Autor:
Matthew D. Liptak, Amanda B. Graves, Angelina Iniguez, Alex Chao, Robert P. Morse, Celia W. Goulding
Publikováno v:
Inorganic Chemistry
Inorganic chemistry, vol 53, iss 12
Graves, AB; Morse, RP; Chao, A; Iniguez, A; Goulding, CW; & Liptak, MD. (2014). Crystallographic and spectroscopic insights into heme degradation by mycobacterium tuberculosis MhuD. Inorganic Chemistry, 53(12), 5931-5940. doi: 10.1021/ic500033b. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/3g78f2wt
Inorganic chemistry, vol 53, iss 12
Graves, AB; Morse, RP; Chao, A; Iniguez, A; Goulding, CW; & Liptak, MD. (2014). Crystallographic and spectroscopic insights into heme degradation by mycobacterium tuberculosis MhuD. Inorganic Chemistry, 53(12), 5931-5940. doi: 10.1021/ic500033b. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/3g78f2wt
Mycobacterium heme utilization degrader (MhuD) is a heme-degrading protein from Mycobacterium tuberculosis responsible for extracting the essential nutrient iron from host-derived heme. MhuD has been previously shown to produce unique organic product
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11768dba2c212a88f07d906c759fca22
https://doi.org/10.1021/ic500033b
https://doi.org/10.1021/ic500033b
Autor:
Celia W. Goulding, Christine A. Harmston, Amanda B. Graves, Nicholas Chim, Heidi Contreras, Angelina Iniguez, Cedric P. Owens, Matthew D. Liptak
Publikováno v:
Journal of Biological Chemistry. 288:21714-21728
Mycobacterium tuberculosis is the causative agent of tuberculosis, which is becoming an increasingly global public health problem due to the rise of drug-resistant strains. While residing in the human host, M. tuberculosis needs to acquire iron for i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f521ce885c4348aabd34d8989245ce90
https://doi.org/10.1074/jbc.m113.453076
https://doi.org/10.1074/jbc.m113.453076
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 45(28)
Correction for ‘Dynamic ruffling distortion of the heme substrate in non-canonical heme oxygenase enzymes’ by Amanda B. Graves et al., Dalton Trans., 2016, 45, 10058–10067.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39ff769a98e67780bf54c6b0b05e7447
https://pubmed.ncbi.nlm.nih.gov/27376412
https://pubmed.ncbi.nlm.nih.gov/27376412
Publikováno v:
Dalton transactions (Cambridge, England : 2003). 45(24)
Recent work by several groups has established that MhuD, IsdG, and IsdI are non-canonical heme oxygenases that induce significant out-of-plane ruffling distortions of their heme substrates enroute to mycobilin or staphylobilin formation. However, cle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a89b308ba258aa9dda79ade4ae0bbdf0
https://pubmed.ncbi.nlm.nih.gov/27273757
https://pubmed.ncbi.nlm.nih.gov/27273757