The Kinetics of Conformational Changes in Hemoglobin, Studied by Laser Photolysis | Zendy

Bernard Alpert | Zendy; R. Banerjee | Zendy; Lars Lindqvist | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

The Kinetics of Conformational Changes in Hemoglobin, Studied by Laser Photolysis

Author(s) -

Bernard Alpert,

R. Banerjee,

Lars Lindqvist

Publication year - 1974

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.71.2.558

Subject(s) - photodissociation , kinetics , carbon monoxide , chemistry , hemoglobin , heme , dissociation (chemistry) , photochemistry , hemeprotein , oxygen , kinetic energy , biochemistry , catalysis , organic chemistry , physics , quantum mechanics , enzyme

Photolysis of carbon monoxide and oxygen derivatives of hemoglobin by a short laser pulse produces a transient species that rapidly decays to normal deoxyhemoglobin. The effect, which is also observed on single chain proteins and on noncooperative aggregated forms, has been interpreted as corresponding to structural changes in the heme pocket on ligand dissociation. The decay of the transient species follows first-order kinetics with constants ranging from 0.8 to 1.8 x 10(7) sec(-1). In cooperative hemoglobins, the kinetic constants are pH-dependent, though remaining first- or pseudo first-order at all wavelengths. This shows the close linkage of tertiary and quaternary structure changes in normal hemoglobin.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research