Rate Constants for Addition of a Primary Alkyl Radical to Carbon Monoxide

1995 ◽  
Vol 60 (23) ◽  
pp. 7384-7385 ◽  
Author(s):  
Kiyoto Nagahara ◽  
Ilhyong Ryu ◽  
Nobuaki Kambe ◽  
Mitsuo Komatsu ◽  
Noboru Sonoda
Keyword(s):  
Carbon Monoxide ◽  
Rate Constants ◽  
Alkyl Radical ◽  
Rate Constants For Addition

ChemInform Abstract: Rate Constants for Addition of a Primary Alkyl Radical to Carbon Monoxide.

ChemInform ◽  
2010 ◽  
Vol 27 (14) ◽  
pp. no-no
Author(s):  
K. NAGAHARA ◽  
I. RYU ◽  
N. KAMBE ◽  
M. KOMATSU ◽  
N. SONODA
Keyword(s):  
Carbon Monoxide ◽  
Rate Constants ◽  
Alkyl Radical ◽  
Rate Constants For Addition

Rate constants of the reaction of fluorine atoms with carbon monoxide

1975 ◽  
Vol 3 (2) ◽  
pp. 205-207 ◽  
Author(s):  
V. S. Arutyunov ◽  
S. N. Buben ◽  
A. M. Chaikin
Keyword(s):  
Carbon Monoxide ◽  
Rate Constants

The analysis of muonium hyperfine interaction measurements of thermal rate constants for addition reactions

1991 ◽  
Vol 94 (4) ◽  
pp. 2794-2806 ◽  
Author(s):  
Ronald J. Duchovic ◽  
Albert F. Wagner ◽  
Ralph Eric Turner ◽  
David M. Garner ◽  
Donald G. Fleming
Keyword(s):  
Hyperfine Interaction ◽  
Rate Constants ◽  
Addition Reactions ◽  
Thermal Rate Constants ◽  
Muonium Hyperfine ◽  
Rate Constants For Addition

Rate constants for energy transfer in carbon monoxide

2000 ◽  
Vol 113 (12) ◽  
pp. 4869 ◽  
Author(s):  
Cecilia Coletti ◽  
Gert D. Billing
Keyword(s):  
Carbon Monoxide ◽  
Energy Transfer ◽  
Rate Constants

Rate constants and Arrhenius parameters for the reaction of a primary alkyl radical with tributylgermanium hydride

1983 ◽  
Vol 105 (11) ◽  
pp. 3578-3580 ◽  
Author(s):  
J. Lusztyk ◽  
B. Maillard ◽  
D. A. Lindsay ◽  
K. U. Ingold
Keyword(s):  
Rate Constants ◽  
Alkyl Radical ◽  
Arrhenius Parameters

scholarly journals Analysis of the contribution of the globin and reductase domains to the ligand-binding properties of bacterial haemoglobins

2007 ◽  
Vol 407 (1) ◽  
pp. 15-22 ◽  
Author(s):  
Judith Farrés ◽  
Susanna Burckhardt-Herold ◽  
Jan Scherrer ◽  
Alexander D. Frey ◽  
Pauli T. Kallio
Keyword(s):  
Nitric Oxide ◽  
Carbon Monoxide ◽  
Fusion Protein ◽  
Ligand Binding ◽  
Rate Constants ◽  
Ralstonia Eutropha ◽  
Solvent Accessibility ◽  
Truncated Form ◽  
Binding Properties ◽  
Reductase Domain

Bacterial Hbs (haemoglobins), like VHb (Vitreoscilla sp. Hb), and flavoHbs (flavohaemoglobins), such as FHP (Ralstonia eutropha flavoHb), have different autoxidation and ligand-binding rates. To determine the influence of each domain of flavoHbs on ligand binding, we have studied the kinetic ligand-binding properties of oxygen, carbon monoxide and nitric oxide to the chimaeric proteins, FHPg (truncated form of FHP comprising the globin domain alone) and VHb-Red (fusion protein between VHb and the C-terminal reductase domain of FHP) and compared them with those of their natural counterparts, FHP and VHb. Moreover, we also analysed polarity and solvent accessibility to the haem pocket of these proteins. The rate constants for the engineered proteins, VHb-Red and FHPg, do not differ significantly from those of their natural counterparts, VHb and FHP respectively. Our results suggest that the globin domain structure controls the reactivity towards oxygen, carbon monoxide and nitric oxide. The presence or absence of a reductase domain does not affect the affinity to these ligands.

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