Binding interaction of hypocrellin B to myoglobin: A spectroscopic and computational study

Interaction of the synthetic antithrombotic peptide P10 with thrombin: a spectroscopy study

“…The interaction under dynamic quenching increases the number of effective collisions and enhances energy transfer, thus increasing the quenching constant of the uorescent material as the temperature increases. 26,30 The ratio of F 0 /F was linear with the concentration of P10, and the slope of the quenching curve at 290 K was higher than that at 310 K (Fig. 2B).…”

Multifaceted Analysis of the Noncovalent Interactions of Myoglobin with Finely Tuned Gemini Surfactants: A Comparative Study

“…The absorption spectrum of Mb exhibits two major peaks in the range of 200–700 nm, respectively, as shown in Figure . The peak in the range of 250–300 nm arises mainly due to π–π* transitions and is concerned with the polarity of the microenvironment around aromatic residues and the latter peak at ∼409 nm is the porphyrin-Soret band, which originates due to the interaction of heme with well-defined tertiary structure of the protein, followed by less intense bands at 504 nm (Q-band) and 630 nm (charge-transfer band). These bands are characteristic of a six-coordinated high-spin (6-cHS) heme with a histidine residue (His-93) and a water molecule bound at the fifth and sixth coordination sites of the Fe atom, respectively .…”

Targeting the heme proteins hemoglobin and myoglobin by janus green blue and study of the dye–protein association by spectroscopy and calorimetry

“…Recently, a number of studies on small molecules binding to Hb have been reported [5][6][7][8][9][10][11][12][13][14][15] while studies on the binding of small molecules to Mb are scarce. [16][17][18][19] Janus green B (JGB) (3-(diethylamino-7-(4-dimethyl amino phenyl azo)-5-phenylphenazinium chloride)) (Fig. 1) is a basic phenazinium dye having anti malarial potency 20 and known to behave as an accurate inhibitor for specic supravital staining of mitochondria.…”