Identification and analysis of the perturbed cΠ3(v=1)–XΣ+1 and kΠ3(v=5)–XΣ+1 absorption bands of carbon monoxide

2005 ◽  
Vol 123 (23) ◽  
pp. 234302 ◽  
Author(s):  
Jacob Baker ◽  
Françoise Launay
Keyword(s):  
Carbon Monoxide ◽  
Absorption Bands

scholarly journals The porphyrin of component c of cytochrome and its relationship to other porphyrins

1930 ◽  
Vol 107 (751) ◽  
pp. 286-292 ◽  
Keyword(s):  
Carbon Monoxide ◽  
Absorption Spectrum ◽  
Living Cells ◽  
Yeast Cells ◽  
Iron Porphyrin ◽  
Cell Component ◽  
Absorption Bands ◽  
Component C

Of the hæmatin compounds present in the cell, component c of cytochrome alone can be readily obtained in solution by extraction with water of either dry or acetone yeast (Keilin, 1925). Recently a method for extracting and concentrating this pigment from yeast has been described, and it was found that the component c thus obtained has the same properties as it has in intact living cells or in the extracts of dry of acetone yeast cells (Keilin, 1930, pp. 421-423). It was shown previously that cytochrome c is a hæmochromogen which differs from the usual hæmochromogen compounds in two important properties, namely, in not being autoxidisable and in not forming a carbon monoxide compound. It was also shown that, without changing it absorption spectrum, the component c can be easily modified in such a way as to show the properties of an ordinary hæmochromogen (Keilin, 1925, 1926). As the various hæmochromogens obtained from cytochrome c have the positions of the absorption bands very different from those of protohæmochromogens it was clear that the iron-porphyrin portion of its molecule is completely different from the ordinary protohæmatin. A series of facts discussed in previous papers suggested, however, that cytochrome originated from the ordinary protohæmatin which is also present in all cells of aerobic organisms. The object of the experiments described in this paper is the study of the porphyrin portion of cytochrome c and its relationship to other prophyrins, especially to protoporphyrin.

FORBIDDEN TRANSITIONS IN DIATOMIC MOLECULES: IV. THE a′3Σ+ ← XlΣ+ AND e3Σ− ← X1Σ+ ABSORPTION BANDS OF CARBON MONOXIDE

1955 ◽  
Vol 33 (12) ◽  
pp. 757-772 ◽  
Author(s):  
G. Herzberg ◽  
T. J. Hugo
Keyword(s):  
Carbon Monoxide ◽  
Diatomic Molecules ◽  
Electronic Transitions ◽  
Absorption Bands ◽  
Unusual Structure ◽  
Precise Data ◽  
Forbidden Transitions ◽  
Perturbation Data ◽  
Vibrational Constants ◽  
Heteronuclear Molecules

Two examples of forbidden electronic transitions in heteronuclear molecules, 3Σ+ – 1Σ+ and 3Σ− – 1Σ+, are studied in the spectrum of the CO molecule. The bands have been obtained in absorption in the region 1750 to 1230 Å with absorbing paths up to 400 cm-atm., using the fourth and fifth orders of a 3 meter vacuum spectrograph. In most of the 3Σ+ – 1Σ+ bands all four predicted branches are observed. For the 3Σ− – 1Σ+ bands, a somewhat unusual structure is predicted: two branches of O and S form and three branches of Q form. In the best-resolved bands, four branches are observed which closely fit the predicted branches, two of the Q branches being very nearly coincident and unresolved in the present spectra. The rotational and vibrational constants of the upper states, a′3Σ+ and e3Σ− of the two band systems have been determined. Some of these data had previously been obtained from perturbations in other band systems of CO. On the whole, the perturbation data agree satisfactorily with the more precise data obtained directly in the present study.

scholarly journals Tracking Africa’s Inferno

2000 ◽  
Vol 122 (12) ◽  
pp. 66-70
Author(s):  
Michael Valenti
Keyword(s):  
Carbon Monoxide ◽  
Field Experiment ◽  
South African ◽  
Correlation Spectroscopy ◽  
The Other ◽  
Absorption Bands ◽  
Infrared Radiance ◽  
Moderate Resolution ◽  
Resolution Imaging ◽  
Aircraft Study

This article focuses on instruments aboard an orbiting satellite and high-flying aircraft study grass fires that straddle a continent. NASA designed its $1.3 billion Terra to be the flagship in a new series of Earth-observing satellites that will study phenomena affecting the climate. The instruments carried by Terra that were most active during the Safari 2000 field experiment were Moderate-Resolution Imaging Spectro-Radiometer (MODIS), Multi-Angle Imaging Spectro-Radiometer (MISR), and Measurements of Pollution in the Troposphere (MOPITT). MOPITT accomplishes its mission by using gas correlation spectroscopy to measure rising and reflected infrared radiance in three absorption bands of carbon monoxide and methane. The Terra’s Safari 2000 observations were augmented by measurements taken by instruments aboard several aircraft, including the high-altitude Lockheed-Martin ER-2 that NASA flew from Pietersburg, South Africa, as part of the African field experiment. The South African Weather Bureau contributed two Aerocommander 690A aircraft to Safari 2000. One of the twin-engine, turboprop planes was used for aerosol research, while the other one helped validate the carbon monoxide measurements obtained by MOPITT.

HIGH-RESOLUTION SPECTRA AND PHOTOABSORPTION COEFFICIENTS FOR CARBON MONOXIDE ABSORPTION BANDS BETWEEN 94.0 nm AND 100.4 nm

1988 ◽  
Vol 49 (C1) ◽  
pp. C1-37-C1-40 ◽  
Author(s):  
K. YOSHINO ◽  
G. STARK ◽  
P. L. SMITH ◽  
W. H. PARKINSON ◽  
K. ITO
Keyword(s):  
Carbon Monoxide ◽  
High Resolution ◽  
Absorption Bands

Infrared spectra of carbon monoxide chemisorbed on metal films: a comparative study of copper, silver, gold, iron, cobalt and nickel

1970 ◽  
Vol 316 (1525) ◽  
pp. 169-183 ◽  
Keyword(s):  
Carbon Monoxide ◽  
Infrared Spectra ◽  
Noble Metals ◽  
Metal Films ◽  
Absorption Bands ◽  
High Coverage ◽  
Iron Cobalt ◽  
Adsorbed Gas ◽  
Adsorbed Carbon ◽  
Cobalt And Nickel

Infrared spectra have been obtained of carbon monoxide chemisorbed on very thin metal films deposited at 113 K under ultrahigh vacuum conditions. On iron, cobalt and nickel the spectra are similar to those found with silica-supported metals, but the absorption bands appeared only at high coverage, indicating that only a part of the adsorbed gas is responsible for them. On copper, silver and gold the adsorbed carbon monoxide is infrared active at low coverages, with bands at 2105, 2160 and 2110 cm -1 respectively. Only one absorption band occurs on each metal, and on copper and gold the absorbance increases linearly with coverage. The extinction coefficients are 1 x 10 -17 and 2 x 10 -17 molecule -1 cm 2 on copper and gold respectively. The relations between frequency, surface potential and heat of adsorption on the noble metals are discussed in terms of σ- and π-bonding.

scholarly journals Factors affecting the measurement of absorption bands

1913 ◽  
Vol 86 (585) ◽  
pp. 128-140 ◽  
Keyword(s):  
Carbon Monoxide ◽  
Individual Variation ◽  
Diffraction Grating ◽  
Wave Length ◽  
Absorption Bands ◽  
Factors Affecting ◽  
Definite Relationship ◽  
Percentage Saturation ◽  
Length Determination

In a previous paper a method was described by which the percentage saturation of hæmoglobin with carbon monoxide can be estimated. This was done by measuring with a special spectroscope the position of the absorption bands of a solution of blood, since it was found that a definite relationship exists between the percentage saturation with carbon monoxide and the wavelength of the bands. The principle used in the instrument was one first discovered by Zöllner in 1870 and called by him the reversion spectroscope. Two adjacent reversed spectra were obtained by passing beams through a slit suitably placed in relation to a reflecting prism and a replica diffraction grating, optical means being employed for shifting one of the spectra laterally, so that corresponding points in the spectra might be adjusted into line. Since first describing the method I have been able to investigate more thoroughly its accuracy both in my own hands and also in those of other observers. Two different classes of phenomena will receive attention, both of which tend to introduce complications in the use of the method when absolute values for the percentage saturation with carbon monoxide are required. These are:— ( a ) Variations in wave-length determinations made from time to time by same observer on different samples of blood (personal variation). ( b ) Variations in wave-length determination by different observers on same sample of blood (individual variation).

Rotational analysis of the forbidden d3 Δi ← X1Σ+ absorption bands of carbon monoxide

1970 ◽  
Vol 48 (24) ◽  
pp. 3004-3015 ◽  
Author(s):  
G. Herzberg ◽  
T. J. Hugo ◽  
S. G. Tilford ◽  
J. D. Simmons
Keyword(s):  
Carbon Monoxide ◽  
High Resolution ◽  
Intensity Distribution ◽  
Vacuum Ultraviolet ◽  
Ultraviolet Region ◽  
Rotational Analysis ◽  
Absorption Bands ◽  
Local Perturbations ◽  
Vacuum Ultraviolet Region ◽  
Π State

The forbidden d3Δi–X1Σ+ transition of CO has been observed in absorption at high resolution in the vacuum ultraviolet region. The intensity distribution in the rotational structure of the observed bands is in conformity with the assumption that the transition occurs on account of the interaction between the d3Δ state and a 1Π state, presumably the A1Π state. Thirteen bands of the d–X system have been analyzed yielding more extensive rotational data for the d3Δi state than were previously known. A discussion of the local perturbations in the d state by the A1Π and a3Π states is included.

scholarly journals SPECTROSCOPY OF CATALASE

1937 ◽  
Vol 20 (4) ◽  
pp. 631-648 ◽  
Author(s):  
Kurt G. Stern
Keyword(s):  
Carbon Monoxide ◽  
Ferric Iron ◽  
Reducing Agents ◽  
Ultraviolet Region ◽  
Absorption Bands ◽  
Main Absorption Band ◽  
Nitrogen Bases ◽  
Nitrogenous Substances ◽  
The Stability ◽  
Blood Pigment

Catalase is resistant to oxidizing agents; e.g., ferricyanide. It is also resistant to reducing agents; e.g., catalytically activated hydrogen, hydrosulfite, ferrotartrate, cysteine. The hemin group of the enzyme will combine with cyanide, sulfides, nitric oxide, fluoride. It will not combine with carbon monoxide. Catalase is therefore a ferric complex. The stability of the ferric iron in the enzyme toward reducing agents is not due to the structure of the porphyrin with which it is combined. This porphyrin is the protoporphyrin of the blood pigment. In combination with globin (methemoglobin) the ferric iron is readily reduced by the same reagents which have no effect on catalase. The stability of the ferric iron in the enzyme is therefore due to the protein component. It may be that the type of hematin-protein linkage in catalase is the reason for this phenomenon. The suggestion of Bersin (31), that sulfur may participate in this linkage, is interesting but, as yet, has no experimental basis. Hydrazine or pyridine and hydrosulfite convert catalase into hemochromogens containing ferrous iron. But in these hemochromogens the hematin is no longer attached to the protein. This has been replaced by the nitrogenous bases hydrazine and pyridine. Both hemochromogens combine reversibly with carbon monoxide. Photo-dissociation has only been demonstrated in the case of the pyridine hemochromogen. The positions of the absorption bands of catalase and its derivatives are listed in Table II. The main absorption band (Soret's band) of hemin complexes with nitrogenous substances (nitrogen bases, proteins) is situated at the border between the visible and the ultraviolet region of the spectrum. It has now been found that the spectrum of purified liver catalase has a well defined maximum of high extinction in this range, at 409 mµ. This is further evidence for the hemin nature of the enzyme.

scholarly journals Global carbon monoxide as retrieved from SCIAMACHY by WFM-DOAS

2004 ◽  
Vol 4 (3) ◽  
pp. 2805-2837 ◽  
Author(s):  
M. Buchwitz ◽  
R. de Beek ◽  
K. Bramstedt ◽  
S. Noël ◽  
H. Bovensmann ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Near Infrared ◽  
Weighting Function ◽  
Lower Troposphere ◽  
Quantitative Information ◽  
Scaling Factor ◽  
Retrieval Algorithm ◽  
Absorption Bands ◽  
Spectral Fitting ◽  
Data Product

Abstract. Vertical columns of CO have been retrieved from SCIAMACHY/ENVISAT short wave/near infrared (~2.3µm) nadir spectra using the Weighting Function Modified (WFM) DOAS retrieval algorithm. WFM-DOAS has been applied to a small spectral fitting window located in SCIAMACHY's channel 8 (~2365 nm) covering four CO absorption lines. The focus of this paper is to demonstrate that quantitative information on carbon monoxide (CO) on a global scale can be retrieved from SCIAMACHY. It is shown that plumes of CO resulting from, e.g. biomass burning in Africa, are clearly detectable with SCIAMACHY. The SCIAMACHY CO columns are in good agreement with the CO column data product of MOPITT (V3). For example, the correlation between SCIAMACHY and MOPITT CO columns for cloud free pixels over land is typically in the range r=0.4–0.7, where r is the correlation coefficient. In order to retrieve good CO columns it was necessary to improve the calibration of the SCIAMACHY nadir spectra. Nevertheless, there is still room for significant improvement. The fit residuals, for example, are dominated by stable and systematic spectral artifacts on the order of the weak CO lines. These artifacts are most pronounced in spectral regions of strong overlapping methane and water vapour absorption bands. They might result from spectrometer slit function uncertainties. The CO columns of the WFM-DOAS Version 0.4 CO column data product presented in this paper have been multiplied by a constant and ground scene independent scaling factor of 0.5 to quantitatively adjust the WFM-DOAS retrieved CO columns to the MOPITT CO data. If and how this scaling factor is influenced by SCIAMACHYs much higher sensitivity to the lower troposphere and boundary layer CO and/or by the currently not perfect spectral fitting needs further investigation.

scholarly journals RESPIRATION AND PROTEIN SYNTHESIS IN ESCHERICHIA COLI MEMBRANE-ENVELOPE FRAGMENTS

1970 ◽  
Vol 46 (1) ◽  
pp. 114-129 ◽  
Author(s):  
Richard W. Hendler ◽  
N. Nanninga
Keyword(s):  
Escherichia Coli ◽  
Carbon Monoxide ◽  
Electron Transport ◽  
Electron Transport Chain ◽  
Wave Length ◽  
Spectrophotometric Analysis ◽  
Difference Spectra ◽  
Absorption Bands ◽  
Optical Extinction ◽  
Transport Chain

The membranous nature of pellets obtained from broken Escherichia coli spheroplasts by successive centrifugation at 3500 g (P1), 20,000 g (P2), and 105,000 g (P3), has been established by electron microscopy. Spectrophotometric analysis has shown that about 90% of the cytochromes are concentrated in the particulate fractions. The crude ribosomal pellet (P3) contained as much of the total cytochromes as did the pellet obtained at 20,000 g (P2). The high cytochrome content of P3 is consistent with its high oxidative activity (1) and the presence of membrane vesicles in this fraction. Analysis at 77°K intensified the optical extinction of all the cytochrome absorption bands, but the degree of intensification was not uniform for each fraction nor for each band within a given fraction. Carbon monoxide had little or no inhibiting effect on NADH oxidation. Reduced plus carbon monoxide difference spectra yielded artifactual absorption bands in the wave length regions where reduced vs. oxidized absorption bands normally occur. Succinate and NADH, either together or separately, reduced nearly all of the cytochromes, indicating that the cytochrome portion of the electron-transport chain is shared by both substrates. A tentative formulation of the electron-transport chain is presented.

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