Electronic state of iron in the oxygen and carbon monoxide adducts of heme proteins

1975 ◽  
Vol 63 (8) ◽  
pp. 3284-3286 ◽  
Author(s):  
A. S. Koster
Keyword(s):  
Carbon Monoxide ◽  
Electronic State ◽  
Heme Proteins

scholarly journals The flame spectrum of carbon monoxide

1940 ◽  
Vol 176 (967) ◽  
pp. 505-521 ◽  
Keyword(s):  
Carbon Dioxide ◽  
Carbon Monoxide ◽  
Electronic State ◽  
Excited Electronic State ◽  
Combustion Process ◽  
Wave Number ◽  
Band Spectrum ◽  
Liquid Form ◽  
Triangular Form ◽  
Reduced Pressure

The spectrum of the flame of carbon monoxide burning in air and in oxygen at reduced pressure has been photographed on plates of high contrast which display the band spectrum clearly above the continuous background. Greater detail has been obtained than has been recorded previously and new measurements are given. The structure of the spectrum has been studied systematically. It is shown that the bands occur in pairs with a separation of about 60 cm. -1 , this separation being due probably to the rotational structure. Various wave-number differences are found to occur frequently, and many of the strong bands are arranged in arrays using intervals of 565 and 2065 cm. -1 . The possible origin of the spectrum is discussed. The choice of emitter is limited to a polyatomic oxide of carbon, of which carbon dioxide is the most likely. The spectrum of the suboxide C 3 O 2 shows some resemblance to the flame bands, but this molecule is improbable as the emitter on other grounds. A peroxide C0 3 is also a possibility, but no evidence for the presence of this has been obtained from experiments on the slow combustion of carbon monoxide. Carbon dioxide in gaseous or liquid form is transparent through the visible and quartz ultra-violet, and the flame bands are not obtained from CO 2 in discharge tubes. Comparison with the Schumann-Runge bands of oxygen shows that it is possible that the flame bands may form part of the absorption band system of CO 2 which is known to exist below 1700 A if there is a big change in shape or size of the molecule in the two electronic states. The electronic energy levels of CO 2 are discussed. Since normal CO 2 is not built up from normal CO and oxygen, an electronic rearrangement of the CO 2 must occur after the combustion process. Mulliken has suggested that the molecule in the first excited electronic state, corresponding to absorption below 1700 A, may have a triangular form. The frequencies obtained from the flame bands are compared with the infra-red frequencies of CO 2 . The 565 interval may be identified with the transverse vibration v 2 , indicating that the excited electronic state is probably triangular in shape. The 2065 interval cannot, however, be identified with the asymmetric vibration v 3 with any certainty. If the excited electronic state of CO 2 is triangular, then molecules formed during the combustion by transitions from this level to the ground state may be “vibrationally activated”. This is probably the reason for many of the peculiarities of the combustion of carbon monoxide.

Carbon Monoxide Binding by de Novo Heme Proteins Derived from Designed Combinatorial Libraries

2001 ◽  
Vol 123 (10) ◽  
pp. 2109-2115 ◽  
Author(s):  
David A. Moffet ◽  
Martin A. Case ◽  
John C. House ◽  
Kathleen Vogel ◽  
Robert D. Williams ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Heme Proteins ◽  
De Novo ◽  
Combinatorial Libraries ◽  
Carbon Monoxide Binding

Neopterin, Dihydroneopterin, Tetrahydroneopterin: Different Structures-Increasing Capacity Cleaving the Porphyrin in Heme Proteins

Pteridines ◽  
2002 ◽  
Vol 13 (4) ◽  
pp. 115-120 ◽  
Author(s):  
Renate Horejsi ◽  
Reinhard Möller ◽  
Erwin Tafeit ◽  
Gilbert Reibnegger
Keyword(s):  
Carbon Monoxide ◽  
Heme Proteins ◽  
Interferon Γ ◽  
Heme Iron ◽  
Oxygen Species ◽  
Subsequent Generation ◽  
Biological Stability ◽  
Human Macrophages ◽  
Non Heme Iron ◽  
Hydroxide Radicals

Abstract Neopterin, 7,8-dihydroneopterin and 5,6,7,8-terahydroneopterm are secreted by human macrophages after activation by interferon-γ. The biological stability of the reduced pterins is less than one hour and therefore distinctly lower than that of neopterin. Ptendme derivatives are known to act as enhancers as well as scavengers of radical mediated processes. The effects of the three pteridines were investigated on hemoglobin and myoglobin, biomolecules that generate reactive oxygen species themselves. The amounts of liberated carbon monoxide and non heme iron stemming from the cleaved porphyrin were quantified. Iron and carbon monoxide were yielded at equimolar concentrations with a con-elation coefficients greater 0.9. Dihydroneopterin and tetrahydroneopterin were assumed to reduce the heme iron in intact heme molecules creating the conditions for adducting carbon monoxide and additionally the subsequent generation of hydroxide radicals via autooxidation. The effect of neopterin under these experimental concentrations was rather weak.

scholarly journals 3P096 Preparation of myoglobin mutants exhibiting preferential binding of oxygen over carbon monoxide(02. Heme proteins,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014))

2014 ◽  
Vol 54 (supplement1-2) ◽  
pp. S264
Author(s):  
Ryu Nishimura ◽  
Daichi Matsumoto ◽  
Tomokazu Shibata ◽  
Sachiko Yanagisawa ◽  
Takashi Ogura ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Annual Meeting ◽  
Heme Proteins ◽  
Biophysical Society ◽  
Preferential Binding

The partial pressure of carbon monoxide in human tissues calculated using a parallel capillary-tissue cylinder model

2018 ◽  
Vol 124 (3) ◽  
pp. 761-768 ◽  
Author(s):  
Ronald F. Coburn
Keyword(s):  
Carbon Monoxide ◽  
Heme Proteins ◽  
Toxic Effects ◽  
Human Tissues ◽  
Co Poisoning ◽  
Tissue Model ◽  
Future Studies ◽  
Cylinder Model ◽  
The Mean

Tissue PCOvalues have not been previously estimated under conditions where the blood carboxyhemoglobin % saturation ([COHb]) is at a normal level or increased. Tissue PCOvalues are not known for conditions when [COHb] is increased during CO therapy or during CO poisoning. Using a modified Krogh parallel capillary-tissue model, mean tissue PCOwas calculated for when [COHb] was 1, 5, 10, and 15% saturation, relevant to CO therapy, and 20, 30, and 40% saturation, relevant to CO poisoning. Calculations were made for the time during which CO was being inhaled, after cessation of CO uptake, and for different O2extractions from blood flowing in the model capillary. The T1/2of relevant CO reactions was used in these calculations. When the [COHb] increased to 5 to 10% saturation, mean tissue PCOvalues increased to 500 to 1,100% of values when the [COHb] was 1% saturation. When the [COHb] increased to 20 to 40% saturation, mean tissue PCOvalues increased to 2,300 to 5,700% of the 1% saturation value. Results indicate the utility of the modified Krogh model in furthering understanding the physiology of determinants of tissue PCOand should facilitate future studies of in vivo CO binding to different extravascular heme proteins during CO therapy and during CO poisoning.NEW & NOTEWORTHY Tissue PCOlevels resulting from carboxyhemoglobin concentrations achieved during CO therapy or during CO poisoning have not been previously estimated. Results published here show that at carboxyhemoglobin levels achieved during CO therapy there are 500 to 1,100% increases in mean tissue PCOvalues. With carboxyhemoglobin increases associated with toxic effects, there are 2,300 to 5,700% increases in the mean tissue PCO. These differences suggest a basis for understanding the therapeutic and toxic effects of CO.

scholarly journals Vibrational Dynamics of Carbon Monoxide at the Active Sites of Mutant Heme Proteins†

1996 ◽  
Vol 100 (29) ◽  
pp. 12100-12107 ◽  
Author(s):  
Jeffrey R. Hill ◽  
Dana D. Dlott ◽  
C. W. Rella ◽  
Kristen A. Peterson ◽  
Sean M. Decatur ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Heme Proteins ◽  
Active Sites ◽  
Vibrational Dynamics
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