Source 1review2007Photosynthesis Research
Toolkit/Mössbauer spectroscopy
Mössbauer spectroscopy
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
FX has been identified in HbRC cores by EPR and Mössbauer spectroscopy, and shown to be a [4Fe-4S]1+,2+ cluster with a ground spin state of S=3/2.
Usefulness & Problems
Why this is useful
Mössbauer spectroscopy is used in the review abstract as part of the evidence identifying FX in HbRC cores.; characterizing iron-sulfur cluster identity in heliobacterial reaction-center cores
Source:
Mössbauer spectroscopy is used in the review abstract as part of the evidence identifying FX in HbRC cores.
Source:
characterizing iron-sulfur cluster identity in heliobacterial reaction-center cores
Problem solved
It helps characterize the iron-sulfur nature of FX and supports its assignment as a [4Fe-4S] cluster.; supports assignment of FX as a [4Fe-4S] cluster with defined spin properties
Source:
It helps characterize the iron-sulfur nature of FX and supports its assignment as a [4Fe-4S] cluster.
Source:
supports assignment of FX as a [4Fe-4S] cluster with defined spin properties
Problem links
supports assignment of FX as a [4Fe-4S] cluster with defined spin properties
LiteratureIt helps characterize the iron-sulfur nature of FX and supports its assignment as a [4Fe-4S] cluster.
Source:
It helps characterize the iron-sulfur nature of FX and supports its assignment as a [4Fe-4S] cluster.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
electronic/spin-state characterization of iron-sulfur clustersspectroscopic detection of iron-containing cofactorsTechniques
Functional AssayTarget processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: sensor
Its use requires Mössbauer instrumentation and appropriate iron-containing HbRC samples.; requires Mössbauer spectroscopy capability and suitable HbRC core samples
the abstract does not provide methodological detail or broader scope beyond FX characterization
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
A low-molecular-mass polypeptide containing the terminal FA and FB iron-sulfur clusters was identified in the heliobacterial reaction center and named PshB.
the low molecular mass polypeptide that contains the terminal FA and FB iron-sulfur clusters has been identified... The gene was named 'pshB' and the protein 'PshB'
FX in heliobacterial reaction-center cores was identified by EPR and Mössbauer spectroscopy as a [4Fe-4S]1+,2+ cluster with a ground spin state of S=3/2.
FX has been identified in HbRC cores by EPR and Mössbauer spectroscopy, and shown to be a [4Fe-4S]1+,2+ cluster with a ground spin state of S=3/2.
ground spin state S=3/2
Removal of the FA/FB-containing polypeptide changes flash-induced kinetics from 75 ms to 15 ms, supporting assignment of the 75 ms phase to P798+ [FA/FB]- recombination and the 15 ms phase to P798+ FX- recombination.
The change in the lifetime of the flash-induced kinetics from 75 ms to 15 ms on its removal shows that the former arises from the P798+ [FA/FB]- recombination, and the latter from P798+ FX- recombination.
flash-induced kinetic lifetime 75 msflash-induced kinetic lifetime 15 ms
Expressed PshB can be rebound to isolated heliobacterial reaction-center cores, restoring the 75 ms kinetic phase and light-induced EPR resonances of FA- and FB-.
The expressed protein can be rebound to isolated HbRC cores, thereby regaining both the 75 ms kinetic phase resulting from P798+ [FA/FB]- recombination and the light-induced EPR resonances of FA- and FB-.
restored kinetic phase lifetime 75 ms
Approval Evidence
1 source1 linked approval claimfirst-pass slug m-ssbauer-spectroscopy
FX has been identified in HbRC cores by EPR and Mössbauer spectroscopy, and shown to be a [4Fe-4S]1+,2+ cluster with a ground spin state of S=3/2.
Source:
component identificationsupports
FX in heliobacterial reaction-center cores was identified by EPR and Mössbauer spectroscopy as a [4Fe-4S]1+,2+ cluster with a ground spin state of S=3/2.
FX has been identified in HbRC cores by EPR and Mössbauer spectroscopy, and shown to be a [4Fe-4S]1+,2+ cluster with a ground spin state of S=3/2.
Source:
Comparisons
Source-stated alternatives
The abstract presents EPR spectroscopy as the paired complementary method.
Source:
The abstract presents EPR spectroscopy as the paired complementary method.
Source-backed strengths
used alongside EPR to identify and characterize FX
Source:
used alongside EPR to identify and characterize FX
Compared with EPR spectroscopy
The abstract presents EPR spectroscopy as the paired complementary method.
Shared frame: source-stated alternative in extracted literature
Strengths here: used alongside EPR to identify and characterize FX.
Relative tradeoffs: the abstract does not provide methodological detail or broader scope beyond FX characterization.
Source:
The abstract presents EPR spectroscopy as the paired complementary method.
Ranked Citations
- 1.