[17] Assignment of rate constants for O2 and CO binding to α and β subunits within R- and T-state human hemoglobin

1994 ◽  
pp. 363-386 ◽  
Author(s):  
Antony J. Mathews ◽  
John S. Olson
Keyword(s):  
Rate Constants ◽  
Human Hemoglobin ◽  
Α And Β Subunits ◽  
T State

scholarly journals Rate Constants for O2and CO Binding to the α and β Subunits within the R and T States of Human Hemoglobin

1998 ◽  
Vol 273 (36) ◽  
pp. 23150-23159 ◽  
Author(s):  
Satoru Unzai ◽  
Raymund Eich ◽  
Naoya Shibayama ◽  
John S. Olson ◽  
Hideki Morimoto
Keyword(s):  
Rate Constants ◽  
Human Hemoglobin ◽  
Α And Β Subunits

scholarly journals Towards understanding non-equivalence of α and β subunits within human hemoglobin in conformational relaxation and molecular oxygen rebinding

2021 ◽  
Author(s):  
Sergei V. Lepeshkevich ◽  
Igor V. Sazanovich ◽  
Marina V. Parkhats ◽  
Syargey N. Gilevich ◽  
Boris M. Dzhagarov
Keyword(s):  
Molecular Oxygen ◽  
Absorption Spectroscopy ◽  
Transient Absorption ◽  
Transient Absorption Spectroscopy ◽  
Human Hemoglobin ◽  
Time Resolved ◽  
Conformational Relaxation ◽  
Α And Β Subunits ◽  
Millisecond Laser

Picosecond to millisecond laser time-resolved transient absorption spectroscopy was used to study molecular oxygen (O2) rebinding and conformational relaxation following O2 photodissociation in the α and β subunits within human...

Conformation of the sebacyl β1Lys82–β2Lys82 crosslink in T-state human hemoglobin

1998 ◽  
Vol 30 (3) ◽  
pp. 309-320 ◽  
Author(s):  
Xinhua Ji ◽  
Michael Braxenthaler ◽  
John Moult ◽  
Clara Fronticelli ◽  
Enrico Bucci ◽  
...  
Keyword(s):  
Human Hemoglobin ◽  
T State

A Kinetic Description of Dioxygen Motion within α- and β-Subunits of Human Hemoglobin in the R-State:  Geminate and Bimolecular Stages of the Oxygenation Reaction†

Biochemistry ◽  
2004 ◽  
Vol 43 (6) ◽  
pp. 1675-1684 ◽  
Author(s):  
Sergei V. Lepeshkevich ◽  
Jerzy Karpiuk ◽  
Igor V. Sazanovich ◽  
Boris M. Dzhagarov
Keyword(s):  
Human Hemoglobin ◽  
Kinetic Description ◽  
Α And Β Subunits

Oxygen Entry through Multiple Pathways in T-State Human Hemoglobin

2013 ◽  
Vol 117 (20) ◽  
pp. 6082-6091 ◽  
Author(s):  
Masayoshi Takayanagi ◽  
Ikuo Kurisaki ◽  
Masataka Nagaoka
Keyword(s):  
Human Hemoglobin ◽  
T State

scholarly journals Stabilization of the T-state of human hemoglobin by proflavine, an antiseptic drug

IUBMB Life ◽  
1999 ◽  
Vol 47 (6) ◽  
pp. 991-995 ◽  
Author(s):  
Paolo Ascenzi ◽  
Marco Colasanti ◽  
Mauro Fasano ◽  
Alberto Bertollini
Keyword(s):  
Human Hemoglobin ◽  
T State

Structure and Oxygen Affinity of Crystalline of DesArg141α Human Hemoglobin A in the T State

1995 ◽  
Vol 248 (1) ◽  
pp. 136-150 ◽  
Author(s):  
Jeffrey S. Kavanaugh ◽  
David R. Chafin ◽  
Arthur Arnone ◽  
Andrea Mozzarelli ◽  
Claudio Rivetti ◽  
...  
Keyword(s):  
Oxygen Affinity ◽  
Human Hemoglobin ◽  
Hemoglobin A ◽  
T State

scholarly journals Comment on ‘Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box size’

2019 ◽  
Author(s):  
Vytautas Gapsys ◽  
Bert L. de Groot
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Size Dependence ◽  
Conformational Transitions ◽  
Human Hemoglobin ◽  
Order Of Magnitude ◽  
The Stability ◽  
Dynamics Simulations ◽  
T State

AbstractA recent molecular dynamics investigation into the stability of hemoglobin concluded that the unliganded protein is only stable in the T state when a solvent box is used in the simulations that is ten times larger than what is usually employed. Here, we express three main concerns about that study. In addition, we show that with an order of magnitude more statistics, the reported box size dependence is not reproducible. Overall, no significant effects on the kinetics or thermodynamics of conformational transitions were observed.

scholarly journals Comment on 'Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box size'

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Vytautas Gapsys ◽  
Bert L de Groot
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Size Dependence ◽  
Conformational Transitions ◽  
Human Hemoglobin ◽  
Order Of Magnitude ◽  
The Stability ◽  
Dynamics Simulations ◽  
T State

A recent molecular dynamics investigation into the stability of hemoglobin concluded that the unliganded protein is only stable in the T state when a solvent box is used in the simulations that is ten times larger than what is usually employed (El Hage et al., 2018). Here, we express three main concerns about that study. In addition, we find that with an order of magnitude more statistics, the reported box size dependence is not reproducible. Overall, no significant effects on the kinetics or thermodynamics of conformational transitions were observed.

Modification of separated α and β subunits of human hemoglobin by iron tetrasulfonated phthalocyanine

1983 ◽  
Vol 79 ◽  
pp. 170
Author(s):  
Helena Przywarska-Boniecka ◽  
Lilianna Trynda ◽  
Teresa Kościukiewicz
Keyword(s):  
Human Hemoglobin ◽  
Α And Β Subunits
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