Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin.
about
Dynamic motion and rearranged molecular shape of heme in myoglobin: structural and functional consequencesTrans-substitution of the proximal hydrogen bond in myoglobin: I. Structural consequences of hydrogen bond deletionStructure and Ligand Selection of Hemoglobin II from Lucina pectinataA double mutant of sperm whale myoglobin mimics the structure and function of elephant myoglobinSignificantly enhanced heme retention ability of myoglobin engineered to mimic the third covalent linkage by nonaxial histidine to heme (vinyl) in synechocystis hemoglobinThe stretching frequencies of bound alkyl isocyanides indicate two distinct ligand orientations within the distal pocket of myoglobin.Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility.Proximal influences in two-on-two globins: effect of the Ala69Ser replacement on Synechocystis sp. PCC 6803 hemoglobinModulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements.The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme.Controlling ligand binding in myoglobin by mutagenesis.Multiple active site conformers in the carbon monoxide complexes of trematode hemoglobins.Distal heme pocket conformers of carbonmonoxy derivatives of Ascaris hemoglobin: evidence of conformational trapping in porous sol-gel matrices.Pathway of information transmission from heme to protein upon ligand binding/dissociation in myoglobin revealed by UV resonance raman spectroscopy.Assessing Low Redox Stability of Myoglobin Relative to Rapid Hemin Loss from Hemoglobin.
P2860
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P2860
Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin.
@en
Serine92
@nl
type
label
Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin.
@en
Serine92
@nl
prefLabel
Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin.
@en
Serine92
@nl
P2093
P356
P1433
P1476
Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin
@en
P2093
A J Wilkinson
M S Hargrove
R E Brantley
T E Carver
P304
P356
10.1021/BI00070A023
P407
P577
1993-05-01T00:00:00Z