Circular dichroism and magnetic circular dichroism of reduced molybdenum-iron protein of Azotobacter vinelandii nitrogenase

Biochemistry ◽  
1981 ◽  
Vol 20 (10) ◽  
pp. 2857-2864 ◽  
Author(s):  
P. J. Stephens ◽  
C. E. McKenna ◽  
M. C. McKenna ◽  
H. T. Nguyen ◽  
F. Devlin
Keyword(s):  
Circular Dichroism ◽  
Azotobacter Vinelandii ◽  
Magnetic Circular Dichroism ◽  
Molybdenum Iron Protein ◽  
Iron Protein ◽  
Circular Dichroïsm

Circular dichroism and magnetic circular dichroism of Azotobacter vinelandii ferredoxin I

Biochemistry ◽  
1991 ◽  
Vol 30 (13) ◽  
pp. 3200-3209 ◽  
Author(s):  
P. J. Stephens ◽  
G. M. Jensen ◽  
F. J. Devlin ◽  
T. V. Morgan ◽  
C. D. Stout ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Azotobacter Vinelandii ◽  
Magnetic Circular Dichroism ◽  
Ferredoxin I ◽  
Circular Dichroïsm

scholarly journals E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii

1992 ◽  
Vol 286 (2) ◽  
pp. 361-367 ◽  
Author(s):  
M R Cheesman ◽  
F H A Kadir ◽  
J al-Basseet ◽  
F al-Massad ◽  
J Farrar ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Circular Dichroism ◽  
Azotobacter Vinelandii ◽  
Magnetic Circular Dichroism ◽  
Charge Transfer Band ◽  
Spectroscopic Characterization ◽  
Detectable Effect ◽  
Iron Core ◽  
Circular Dichroïsm

The e.p.r. and magnetic circular dichroism (m.c.d.) spectra of bacterioferritin (BFR) extracted from Pseudomonas aeruginosa and Azotobacter vinelandii have been studied over a wide temperature range down to liquid-helium temperature. The e.p.r. spectra show the presence of low-spin Fe3+ haem with g values of 2.86, 2.32, 1.48 (P. aeruginosa) and 2.88, 2.31, 1.46 (A. vinelandii), in both the presence and absence of the BFR core. Together with evidence from the porphyrin-to-Fe3+ charge-transfer band at 2240 and 2270 nm the axial haem ligands are identified as two methionines. The low-temperature m.c.d. spectra in the region 300-1000 nm of P. aeruginosa and A. vinelandii BFR are identical with one another and unaffected by removal of the iron core. Hence it can be concluded that the presence of the iron core has no detectable effect on the electronic states and on the stereochemistry of the haem group. This was unexpected, in view of the observations by Watt, Frankel, Papaefthymiou, Spartalian & Stiefel [(1986) Biochemistry 25, 4330-4336] that the redox potential of the haem group in A. vinelandii BFR shifts from -475 mV to -225 mV on removal of the core. The e.p.r. spectra of holoBFR show a broad symmetrical derivative-shaped band centred at g = 2.0 which decreases in bandwidth as the temperature is raised. This signal is assigned to the uncompensated electron spins of the iron core.

scholarly journals Soft x-ray absorption spectroscopy and magnetic circular dichroism as operando probes of complex oxide electrolyte gate transistors

2020 ◽  
Vol 116 (20) ◽  
pp. 201905
Author(s):  
Biqiong Yu ◽  
Guichuan Yu ◽  
Jeff Walter ◽  
Vipul Chaturvedi ◽  
Joseph Gotchnik ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Absorption Spectroscopy ◽  
Magnetic Circular Dichroism ◽  
Complex Oxide ◽  
X Ray ◽  
X Ray Absorption ◽  
Circular Dichroïsm ◽  
Oxide Electrolyte

scholarly journals Natural and magnetic circular dichroism spectra of nucleosides: effect of the dynamics and environment

RSC Advances ◽  
2021 ◽  
Vol 11 (14) ◽  
pp. 8411-8419
Author(s):  
Jakub Kaminský ◽  
Valery Andrushchenko ◽  
Petr Bouř
Keyword(s):  
Molecular Dynamics ◽  
Circular Dichroism ◽  
Nucleic Acids ◽  
Electronic Absorption ◽  
Magnetic Circular Dichroism ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm ◽  
Magnetic Circular Dichroism Spectra

Electronic absorption, natural and magnetic circular dichroism spectra of several nucleosides are simulated to understand their dependence on molecular dynamics and environment, their sensitivity to nucleoside pairing and stacking in nucleic acids.

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