Time-Resolved Crystallographic Studies of the Heme Domain of the Oxygen Sensor FixL:  Structural Dynamics of Ligand Rebinding and Their Relation to Signal Transduction†,‡

Biochemistry ◽  
2007 ◽  
Vol 46 (16) ◽  
pp. 4706-4715 ◽  
Author(s):  
Jason Key ◽  
Vukica Šrajer ◽  
Reinhard Pahl ◽  
Keith Moffat
Keyword(s):  
Signal Transduction ◽  
Structural Dynamics ◽  
Oxygen Sensor ◽  
Time Resolved ◽  
Heme Domain ◽  
Ligand Rebinding

scholarly journals Stationary and Time-resolved Resonance Raman Spectra of His77and Met95Mutants of the Isolated Heme Domain of a Direct Oxygen Sensor fromEscherichia coli

2002 ◽  
Vol 277 (36) ◽  
pp. 32650-32658 ◽  
Author(s):  
Akira Sato ◽  
Yukie Sasakura ◽  
Shunpei Sugiyama ◽  
Ikuko Sagami ◽  
Toru Shimizu ◽  
...  
Keyword(s):  
Raman Spectra ◽  
Oxygen Sensor ◽  
Resonance Raman ◽  
Time Resolved ◽  
Fromescherichia Coli ◽  
Heme Domain ◽  
Resonance Raman Spectra

Structural dynamics of P-type ATPase ion pumps

2019 ◽  
Vol 47 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Mateusz Dyla ◽  
Sara Basse Hansen ◽  
Poul Nissen ◽  
Magnus Kjaergaard
Keyword(s):  
Structural Dynamics ◽  
Single Molecule ◽  
New Technologies ◽  
Atp Hydrolysis ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved ◽  
Dynamics Simulations ◽  
Types Of Information ◽  
P Type

Abstract P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field.

Role of Phe113 at the distal side of the heme domain of an oxygen-sensor (Ec DOS) in the characterization of the heme environment

2009 ◽  
Vol 103 (7) ◽  
pp. 989-996 ◽  
Author(s):  
Shinya Ito ◽  
Yasuyuki Araki ◽  
Atsunari Tanaka ◽  
Jotaro Igarashi ◽  
Takehiko Wada ◽  
...  
Keyword(s):  
Oxygen Sensor ◽  
Distal Side ◽  
Heme Domain

scholarly journals Structural dynamics of the Ca2+-ATPase studied by time-resolved infrared spectroscopy

2008 ◽  
Vol 22 (2-3) ◽  
pp. 63-82 ◽  
Author(s):  
Andreas Barth
Keyword(s):  
Infrared Spectroscopy ◽  
Structural Dynamics ◽  
Ground State ◽  
Transfer Reaction ◽  
High Reactivity ◽  
Acetyl Phosphate ◽  
Time Resolved ◽  
Closed Conformation ◽  
Sarcoplasmic Reticulum Membrane ◽  
Time Resolved Infrared Spectroscopy

This review discusses the contribution of time-resolved infrared spectroscopy to the understanding of the Ca2+pump in the sarcoplasmic reticulum membrane of skeletal muscle cells (SERCA1a). The focus is on interactions of the substrate ATP with the ATPase and on the bond parameters of the phosphoenzyme phosphate group. Functional groups throughout the ATP molecule are important for stabilising the closed conformation of the ATP–ATPase complex and for fast phosphorylation of the ATPase. Dissociation of the reaction product ADP after phosphorylation leads to a more open average conformation of the enzyme and does not trigger the transition from the first phosphoenzyme Ca2E1P to the second E2P. The P–O bond between phosphate and aspartyl moieties is weaker in Ca2E1P and E2P than in acetyl phosphate in aqueous solution, which explains the high reactivity of the phosphoenzymes. This ground state property of the phosphoenzymes prepares for a phosphate transfer reaction with dissociative character.

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