Redox Reactivity of a Mononuclear Manganese-Oxo Complex Binding Calcium Ion and Other Redox-Inactive Metal Ions

2018 ◽  
Vol 141 (3) ◽  
pp. 1324-1336 ◽  
Author(s):  
Muniyandi Sankaralingam ◽  
Yong-Min Lee ◽  
Yuliana Pineda-Galvan ◽  
Deepika G. Karmalkar ◽  
Mi Sook Seo ◽  
...  
Keyword(s):  
Metal Ions ◽  
Calcium Ion ◽  
Redox Reactivity

scholarly journals Probing the Role of Divalent Metal Ions in a Bacterial Psychrophilic Metalloprotease: Binding Studies of an Enzyme in the Crystalline State by X-Ray Crystallography

2003 ◽  
Vol 185 (14) ◽  
pp. 4195-4203 ◽  
Author(s):  
Stephanie Ravaud ◽  
Patrice Gouet ◽  
Richard Haser ◽  
Nushin Aghajari
Keyword(s):  
Metal Ions ◽  
Calcium Ions ◽  
Calcium Ion ◽  
Crystalline State ◽  
Zinc Ion ◽  
Binding Studies ◽  
X Ray ◽  
X Ray Crystallography ◽  
Catalytic Zinc

ABSTRACT The psychrophilic alkaline metalloprotease (PAP) produced by a Pseudomonas bacterium isolated in Antarctica belongs to the clan of metzincins, for which a zinc ion is essential for catalytic activity. Binding studies in the crystalline state have been performed by X-ray crystallography in order to improve the understanding of the role of the zinc and calcium ions bound to this protease. Cocrystallization and soaking experiments with EDTA in a concentration range from 1 to 85 mM have resulted in five three-dimensional structures with a distinct number of metal ions occupying the ion-binding sites. Evolution of the structural changes observed in the vicinity of each cation-binding site has been studied as a function of the concentration of EDTA, as well as of time, in the presence of the chelator. Among others, we have found that the catalytic zinc ion was the first ion to be chelated, ahead of a weakly bound calcium ion (Ca 700) exclusive to the psychrophilic enzyme. Upon removal of the catalytic zinc ion, the side chains of the active-site residues His-173, His-179 and Tyr-209 shifted ∼4, 1.0, and 1.6 Å, respectively. Our studies confirm and also explain the sensitivity of PAP toward moderate EDTA concentrations and propose distinct roles for the calcium ions. A new crystal form of native PAP validates our previous predictions regarding the adaptation of this enzyme to cold environments as well as the proteolytic domain calcium ion being exclusive for PAP independent of crystallization conditions.

Fine Control of the Redox Reactivity of a Nonheme Iron(III)–Peroxo Complex by Binding Redox‐Inactive Metal Ions

2016 ◽  
Vol 129 (3) ◽  
pp. 819-823 ◽  
Author(s):  
Seong Hee Bae ◽  
Yong‐Min Lee ◽  
Shunichi Fukuzumi ◽  
Wonwoo Nam
Keyword(s):  
Metal Ions ◽  
Nonheme Iron ◽  
Peroxo Complex ◽  
Redox Reactivity ◽  
Fine Control

Fine Control of the Redox Reactivity of a Nonheme Iron(III)–Peroxo Complex by Binding Redox‐Inactive Metal Ions

2016 ◽  
Vol 56 (3) ◽  
pp. 801-805 ◽  
Author(s):  
Seong Hee Bae ◽  
Yong‐Min Lee ◽  
Shunichi Fukuzumi ◽  
Wonwoo Nam
Keyword(s):  
Metal Ions ◽  
Nonheme Iron ◽  
Peroxo Complex ◽  
Redox Reactivity ◽  
Fine Control

Rare earth metal ions as substitutes for the calcium ion in Bacillus subtilis .alpha.-amylase

Biochemistry ◽  
1971 ◽  
Vol 10 (24) ◽  
pp. 4556-4561 ◽  
Author(s):  
George E. Smolka ◽  
Edward R. Birnbaum ◽  
Dennis W. Darnall
Keyword(s):  
Bacillus Subtilis ◽  
Rare Earth ◽  
Metal Ions ◽  
Rare Earth Metal ◽  
Calcium Ion ◽  
Earth Metal ◽  
Alpha Amylase

scholarly journals Activation of membrane-bound high-affinity calcium ion-sensitive adenosine triphosphatase of human erythrocytes by bivalent metal ions

1975 ◽  
Vol 147 (2) ◽  
pp. 359-361 ◽  
Author(s):  
H Pfleger ◽  
H U Wolf
Keyword(s):  
Metal Ions ◽  
Calcium Ion ◽  
Metal Ion ◽  
Adenosine Triphosphatase ◽  
Erythrocyte Membranes ◽  
Bivalent Metal ◽  
High Affinity ◽  
Human Erythrocyte Membranes ◽  
Bivalent Metal Ions ◽  
Membrane Bound

The Ca2+-sensitive ATPase (adenosine triphosphatase) of human erythrocyte membranes is activated, not only by Ca2+ ions, but also by a series of other bivalent metal ions including Sr2+, Ba2+, Mn2+, Ni2+, Co2+, Cd2+, Cu2+, Zn2+ and Pb2+. The degree of activation is dependent on the radius of the ion rather than on its nature, in contrast with the dissociation constant of the enzyme--metal ion complex.

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