A New Type of Metalloprotein: The Mo Storage Protein from Azotobacter vinelandii Contains a Polynuclear Molybdenum-Oxide Cluster

ChemBioChem ◽  
2005 ◽  
Vol 6 (2) ◽  
pp. 405-413 ◽  
Author(s):  
Dirk Fenske ◽  
Manuel Gnida ◽  
Klaus Schneider ◽  
Wolfram Meyer-Klaucke ◽  
Jörg Schemberg ◽  
...  
Keyword(s):  
Molybdenum Oxide ◽  
Storage Protein ◽  
Azotobacter Vinelandii ◽  
Oxide Cluster ◽  
New Type

scholarly journals Molybdate pumping into the molybdenum storage protein via an ATP-powered piercing mechanism

2019 ◽  
Vol 116 (52) ◽  
pp. 26497-26504 ◽  
Author(s):  
Steffen Brünle ◽  
Martin L. Eisinger ◽  
Juliane Poppe ◽  
Deryck J. Mills ◽  
Julian D. Langer ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Storage Protein ◽  
Large Scale ◽  
Azotobacter Vinelandii ◽  
Current Data ◽  
Nucleophilic Attack ◽  
Valuable Insight ◽  
Similar Reaction ◽  
Α Subunit ◽  
Ump Kinase

The molybdenum storage protein (MoSto) deposits large amounts of molybdenum as polyoxomolybdate clusters in a heterohexameric (αβ)3cage-like protein complex under ATP consumption. Here, we suggest a unique mechanism for the ATP-powered molybdate pumping process based on X-ray crystallography, cryoelectron microscopy, hydrogen-deuterium exchange mass spectrometry, and mutational studies of MoSto fromAzotobacter vinelandii. First, we show that molybdate, ATP, and Mg2+consecutively bind into the open ATP-binding groove of the β-subunit, which thereafter becomes tightly locked by fixing the previously disordered N-terminal arm of the α-subunit over the β-ATP. Next, we propose a nucleophilic attack of molybdate onto the γ-phosphate of β-ATP, analogous to the similar reaction of the structurally related UMP kinase. The formed instable phosphoric-molybdic anhydride becomes immediately hydrolyzed and, according to the current data, the released and accelerated molybdate is pressed through the cage wall, presumably by turning aside the Metβ149 side chain. A structural comparison between MoSto and UMP kinase provides valuable insight into how an enzyme is converted into a molecular machine during evolution. The postulated direct conversion of chemical energy into kinetic energy via an activating molybdate kinase and an exothermic pyrophosphatase reaction to overcome a proteinous barrier represents a novelty in ATP-fueled biochemistry, because normally, ATP hydrolysis initiates large-scale conformational changes to drive a distant process.

Molybdenum Oxide Cluster Ions in the Gas Phase:  Reactions with Small Alcohols

1998 ◽  
Vol 17 (1) ◽  
pp. 25-31 ◽  
Author(s):  
Elena F. Fialko ◽  
Andrey V. Kikhtenko ◽  
Vladimir B. Goncharov
Keyword(s):  
Gas Phase ◽  
Molybdenum Oxide ◽  
Cluster Ions ◽  
Gas Phase Reactions ◽  
Oxide Cluster

Photochromic effect in molybdenum-oxide cluster systems

1999 ◽  
Vol 41 (7) ◽  
pp. 1210-1215 ◽  
Author(s):  
V. N. Andreev ◽  
S. E. Nikitin ◽  
V. A. Klimov ◽  
F. A. Chudnovskii ◽  
S. V. Kozyrev ◽  
...  
Keyword(s):  
Molybdenum Oxide ◽  
Oxide Cluster ◽  
Cluster Systems ◽  
Photochromic Effect

scholarly journals The complete nucleotide sequence of new type cDNA coding for rice storage protein glutelin

1989 ◽  
Vol 17 (8) ◽  
pp. 3289-3289 ◽  
Author(s):  
Fumio Takaiwa ◽  
Shoshi Kikuchi ◽  
Kiyoharu Oono
Keyword(s):  
Nucleotide Sequence ◽  
Storage Protein ◽  
Complete Nucleotide Sequence ◽  
New Type

A new type of molybdenum oxide crystal encapsulated inside a single-walled carbon nanotube

Microscopy ◽  
2012 ◽  
Vol 62 (2) ◽  
pp. 271-282 ◽  
Author(s):  
Ryusuke Sagawa ◽  
Wataru Togashi ◽  
Tomoki Akita ◽  
Yoshizo Takai
Keyword(s):  
Carbon Nanotube ◽  
Molybdenum Oxide ◽  
Single Walled Carbon Nanotube ◽  
Single Walled Carbon ◽  
Oxide Crystal ◽  
New Type
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