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| AUTHOR |
TITLE |
Chen, F.-M.,
Sha, F. |
Circular Dichroic and Kinetic Differentiation of DNA Binding Modes of Distamycin
Biochemistry; 1998; 37(32); 11143-11151. (Article) |
Materials and Methods
Stopped-flow kinetic measurements were made with an Olis RSM-1000 system. |
Chen, F.-M.,
Liu, C. |
Is the Strong Actinomycin D Binding of d(5'CGTCGACG3') the Consequence of End-Stacking?
Biochemistry; 1996; 35(22); 7283-7291 (Article) |
Materials and Methods
Stopped-flow kinetic measurements were made with an Olis RSM-1000 rapid scan spectrophotometer. |
Tegoni, M.,
Silvestrini, M. C.,
Guigliarelli, B.,
Asso, M.,Brunori, M.,
Bertrand, P. |
Temperature-Jump and Potentiometric Studies on Recombinant Wild Type and Y143F and Y254F Mutants of Saccharomyces cerevisiae Flavocytochrome b2: Role of the Driving Force in Intramolecular Electron Transfer Kinetics
Biochemistry; 1998; 37(37); 12761-12771. (Article) |
Materials and Methods
Temperature Jump Experiments:
The absorption spectra recorded during the experiments in the temperature-jump cell fitted to an OLIS modified Cary-14 spectrophotometer were used to directly monitor the heme reduction levels. |
Richter, H. W.,
Cherry, B. R.,
Zook, T. D.,
Koser, G. F. |
Characterization of Species Present in Aqueous Solutions of [Hydroxy(mesyloxy)iodo]benzene and [Hydroxy(tosyloxy)iodo]benzene
Journal of the American Chemical Society; 1997; 119(41); 9614-9623.
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Experimental Materials and Methods
Spectroscopy and Potentiometric Titrations
UV-vis spectroscopic measurements were recorded on a Cary 17 spectrophotometer updated by OLIS, Inc., Bogart, GA, to allow digital recording of spectra. |
Devanathan, S.,
Brudler, R.,
Hessling, B.,
Woo, T. T.,
Gerwert, K.,
Getzoff, E. D.,
Cusanovich, M. A.,
Tollin, G. |
Dual Photoactive Species in Glu46Asp and Glu46Ala Mutants of Photoactive Yellow Protein: A pH-Driven Color Transition
Biochemistry; 1999; 38(41); 13766-13772. |
Materials and Methods
Steady State and Time Resolved Optical Spectroscopy
The dark recovery kinetic experiments for the Glu46Asp mutant were performed either on the diode array spectrophotometer or on an Olis-modified Cary 15 spectrophotometer. In the dark recovery experiments, the protein was first subjected to white light irradiation with a 100 W fiber optic illuminator for 3 min to ensure maximal conversion to the photobleached form; subsequently, the sample was placed in the dark, and absorption spectra were obtained every 30 s. |
Devanathan, S.,
Genick, U. K.,
Canestrelli, I. L.,
Meyer, T. E.,
Cusanovich, M. A.,
Getzoff, E. D.,
Tollin, G. |
New Insights into the Photocycle of Ectothiorhodospira halophila Photoactive Yellow Protein: Photorecovery of the Long-Lived Photobleached Intermediate in the Met100Ala Mutant
Biochemistry; 1998; 37(33); 11563-11568. (Article) |
Materials and Methods
Time Resolved Optical Spectroscopy
A modified Cary-15 spectrophotometer (OLIS Corp., Bogart, GA) was used to follow the dark recovery kinetics. Absorbance changes were determined over a 30-60 min time period after photobleaching the sample, and the data were fit with a single-exponential function using OLIS software. |
Martinez-Julvez, M.,
Hermoso, J.,
Hurley, J. K.,
Mayoral, T.,
Sanz-Aparicio, J.,
Tollin, G.Gomez-Moreno, C.,
Medina, M. |
Role of Arg100 and Arg264 from Anabaena PCC 7119 Ferredoxin-NADP+ Reductase for Optimal NADP+ Binding and Electron Transfer
Biochemistry; 1998; 37(51); 17680-17691. |
Materials and Methods
Spectral Analysis
UV-visible spectra were measured on a Cary-15 (Olis-modified), a Hewlett-Packard 8452 diode array, or a Kontron Uvikon 942 spectrophotometer.
Laser Flash Photolysis Measurements
Digitized kinetic traces were analyzed using a computer fitting routine (Kinfit, Olis Co., Bogart, GA). Generally, four to ten flashes were averaged. Experiments were carried out under pseudo-first-order conditions in which Fd is present in large excess over the dRfH generated by the laser flash (<1 µM). Laser flash-induced kinetic measurements were taken at room temperature. In addition to protein, samples also contained 1 mM EDTA and 95-100 µM dRf in 4 mM potassium phosphate buffer (pH 7.0). The ionic strength of the solution was adjusted using a 5 M NaCl stock solution. Samples were made anaerobic as described previously (11, 31). |
Martinez-Julvez, M.,
Medina, M.,
Hurley, J. K.,
Hafezi, R.,
Brodie, T. B.,
Tollin, G.,
Gomez-Moreno, C. |
Lys75 of Anabaena Ferredoxin-NADP+ Reductase Is a Critical Residue for Binding Ferredoxin and Flavodoxin during Electron Transfer
Biochemistry; 1998; 37(39); 13604-13613. (Article) |
Materials and Methods.
Spectral Analysis
UV-visible spectral analyses were carried out on either a CARY-15 (OLIS-modified), a Hewlett-Packard 8452 diode array, or a Kontron Uvikon 942 spectrophotometer. The spectra were recorded on solutions having protein concentrations ranging from 55 to 77 μM in the visible region (300-620 nm), of 4 μM for the aromatic region, and of 0.7 μM for the far-UV region. Samples were prepared in 20 mM Tris-HCl (pH 7.3) for the visible region and in 1 mM Tris-HCl (pH 8.0) for the aromatic and far-UV regions. Protein and flavin fluorescence were monitored using a Kontron SFM 25 spectrofluorometer interfaced with a personal computer. Solutions for fluorescence measurements contained 4 μM protein in 50 mM Tris-HCl (pH 8.0). |
Medina, M.,
Martinez-Julvez, M.,
Hurley, J. K.,
Tollin, G.,
Gomez-Moreno, C. |
Involvement of Glutamic Acid 301 in the Catalytic Mechanism of Ferredoxin-NADP+ Reductase from Anabaena PCC 7119
Biochemistry; 1998; 37(9); 2715-2728. (Article) |
Laser Flash Photolysis Measurements
Kinetic traces were analyzed using a computer fitting routine (KINFIT, OLIS Co., Bogart, GA). The apparent complex dissociation constant and the limiting first-order rate constant for intracomplex electron transfer were evaluated from these data by a nonlinear least-squares computer-fitting procedure (30). |
Hurley, J. K.,
Weber-Main, A. M.,
Hodges, A. E.,
Stankovich, M. T.,
Benning, M. M.,
Holden, H. M.,
Cheng, H.,
Xia, B.,
Markley, J. L.,
Genzor, C.,
Gomez-Moreno, C.,
Hafezi, R.,
Tollin, G. |
Iron-Sulfur Cluster Cysteine-to-Serine Mutants of Anabaena [2Fe-2S] Ferredoxin Exhibit Unexpected Redox Properties and Are Competent in Electron Transfer to Ferredoxin:NADP+ Reductase
Biochemistry; 1997; 36(49); 15109-15117. (Article) |
Materials and Methods
Digitized kinetic traces were analyzed using a computer fitting routine (Kinfit, OLIS Co., Bogart, GA). |
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