Functional Properties of the Heme Propionates in CytochromecOxidase fromParacoccus denitrificans.Evidence from FTIR Difference Spectroscopy and Site-Directed Mutagenesis†

Biochemistry ◽  
2000 ◽  
Vol 39 (6) ◽  
pp. 1356-1363 ◽  
Author(s):  
Julia Behr ◽  
Hartmut Michel ◽  
Werner Mäntele ◽  
Petra Hellwig
Keyword(s):  
Functional Properties ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Difference Spectroscopy ◽  
Ftir Difference Spectroscopy

scholarly journals Structural basis for the functional properties of the P2X7 receptor for extracellular ATP

2021 ◽  
Author(s):  
Lin-Hua Jiang ◽  
Emily A. Caseley ◽  
Steve P. Muench ◽  
Sébastien Roger
Keyword(s):  
Functional Properties ◽  
P2x7 Receptor ◽  
Site Directed Mutagenesis ◽  
P2x Receptor ◽  
Structural Basis ◽  
Structure Characteristic ◽  
Purinergic Signalling ◽  
Directed Mutagenesis ◽  
Important Mediator ◽  
Receptor Family

AbstractThe P2X7 receptor, originally known as the P2Z receptor due to its distinctive functional properties, has a structure characteristic of the ATP-gated ion channel P2X receptor family. The P2X7 receptor is an important mediator of ATP-induced purinergic signalling and is involved the pathogenesis of numerous conditions as well as in the regulation of diverse physiological functions. Functional characterisations, in conjunction with site-directed mutagenesis, molecular modelling, and, recently, structural determination, have provided significant insights into the structure–function relationships of the P2X7 receptor. This review discusses the current understanding of the structural basis for the functional properties of the P2X7 receptor.

scholarly journals Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin: a study aided by site-directed mutagenesis

1993 ◽  
Vol 296 (3) ◽  
pp. 721-728 ◽  
Author(s):  
A Treffry ◽  
E R Bauminger ◽  
D Hechel ◽  
N W Hodson ◽  
I Nowik ◽  
...  
Keyword(s):  
Iron Uptake ◽  
Iron Oxidation ◽  
Site Directed Mutagenesis ◽  
Iron Core ◽  
Directed Mutagenesis ◽  
Difference Spectroscopy ◽  
Iron Storage ◽  
Ferritin Iron ◽  
Iron Storage Protein

This paper aims to define the role of the threefold intersubunit channels in iron uptake and sequestration processes in the iron-storage protein, ferritin. Iron uptake, measured as loss of availability of Fe(II) to ferrozine (due to oxidation), has been studied in recombinant human H-chain ferritins bearing amino acid substitutions in the threefold channels or ferroxidase centres. Similar measurements with recombinant horse L-chain ferritin are compared. It is concluded that significant Fe(II) oxidation occurs only at the H-chain ferroxidase centres and not in the threefold channels, although this route is used by Fe(II) for entry. Investigations by Mössbauer and u.v.-difference spectroscopy show that part of the iron oxidized by H-chain ferritin returns to the threefold channels as Fe(III). This monomeric Fe(III) can be displaced by addition of Tb(III). Fe(III) also moves into the cavity for formation of the iron-core mineral, ferrihydrite. Iron incorporated into ferrihydrite becomes kinetically inert.

Functional Properties of Human b2-Adrenergic Receptor Polymorphisms

Physiology ◽  
1995 ◽  
Vol 10 (6) ◽  
pp. 265-273 ◽  
Author(s):  
S Liggett
Keyword(s):  
Genetic Polymorphisms ◽  
Functional Properties ◽  
Adrenergic Receptor ◽  
Human Population ◽  
Recombinant Expression ◽  
Receptor Gene ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

The same b2-adrenergic receptor is not expressed throughout the human population;there are at least six different forms of the receptor due to genetic polymorphisms within the coding block of the receptor gene. Site-directed mutagenesis and recombinant expression have shown that some of these variants have distinct pharmacological and biochemical phenotypes.

Sign in / Sign up

Export Citation Format

Share Document