Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.

Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.

Item
http://www.wikidata.org/entity/Q45930929
Covalent heme attachment inSynechocystishemoglobin is required to prevent ferrous heme dissociationStructural analysis of fish versus mammalian hemoglobins: Effect of the heme pocket environment on autooxidation and hemin lossSignificantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobinCharacterization of heme ligation properties of Rv0203, a secreted heme binding protein involved in Mycobacterium tuberculosis heme uptake.Redox reactions of myoglobinDifferential heme release from various hemoglobin redox states and the upregulation of cellular heme oxygenase-1Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reactions with ligands.Folding myoglobin within a sol-gel glass: protein folding constrained to a small volume.Unusual effects of crowders on heme retention in myoglobin.Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH.Why hypothetical protein KPN00728 of Klebsiella pneumoniae should be classified as chain C of succinate dehydrogenase?
P2860

Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.

Item
http://www.wikidata.org/entity/Q45930929
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh-hant
name
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
@en
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
@nl
type
label
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
@en
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
@nl
prefLabel
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
@en
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698