New perspectives on bacterial ferredoxin evolution

1985 ◽  
Vol 22 (1) ◽  
pp. 20-31 ◽  
Author(s):  
David G. George ◽  
Lois T. Hunt ◽  
Lai-Su L. Yeh ◽  
Winona C. Barker
Keyword(s):  
Bacterial Ferredoxin

Synthesis of haptenic C-terminal octapeptides of two cross-reacting bacterial ferredoxin molecules

Biochemistry ◽  
1970 ◽  
Vol 9 (8) ◽  
pp. 1839-1844 ◽  
Author(s):  
Barbara Mitchell ◽  
Julia Gerwing Levy ◽  
Rodney M. Nitz
Keyword(s):  
Bacterial Ferredoxin

Swapping FAD Binding Motifs between Plastidic and Bacterial Ferredoxin-NADP(H) Reductases

Biochemistry ◽  
2011 ◽  
Vol 50 (12) ◽  
pp. 2111-2122 ◽  
Author(s):  
Matías A. Musumeci ◽  
Horacio Botti ◽  
Alejandro Buschiazzo ◽  
Eduardo A. Ceccarelli
Keyword(s):  
Binding Motifs ◽  
Bacterial Ferredoxin ◽  
Fad Binding

scholarly journals Modular origins of biological electron transfer chains

2018 ◽  
Vol 115 (6) ◽  
pp. 1280-1285 ◽  
Author(s):  
Hagai Raanan ◽  
Douglas H. Pike ◽  
Eli K. Moore ◽  
Paul G. Falkowski ◽  
Vikas Nanda
Keyword(s):  
Electron Transfer ◽  
Building Blocks ◽  
Transfer Reactions ◽  
Additional Insight ◽  
Modular Units ◽  
Biological Electron Transfer ◽  
Bacterial Ferredoxin ◽  
Insight Into ◽  
Structural Alignments ◽  
Ancestral Protein

Oxidoreductases catalyze electron transfer reactions that ultimately provide the energy for life. A limited set of ancestral protein-metal modules are presumably the building blocks that evolved into this diverse protein family. However, the identity of these modules and their path to modern oxidoreductases is unknown. Using a comparative structural analysis approach, we identify a set of fundamental electron transfer modules that have evolved to form the extant oxidoreductases. Using transition metal-containing cofactors as fiducial markers, it is possible to cluster cofactor microenvironments into as few as four major modules: bacterial ferredoxin, cytochrome c, symerythrin, and plastocyanin-type folds. From structural alignments, it is challenging to ascertain whether modules evolved from a single common ancestor (homology) or arose by independent convergence on a limited set of structural forms (analogy). Additional insight into common origins is contained in the spatial adjacency network (SPAN), which is based on proximity of modules in oxidoreductases containing multiple cofactor electron transfer chains. Electron transfer chains within complex modern oxidoreductases likely evolved through repeated duplication and diversification of ancient modular units that arose in the Archean eon.

Resonance raman spectroscopic evidence for structural variation among bacterial ferredoxin, HiPIP, and Fe4S4(SCH2Ph)42−*

1975 ◽  
Vol 62 (1) ◽  
pp. 1-6 ◽  
Author(s):  
S-P.W. Tang ◽  
T.G. Spiro ◽  
C. Antanaitis ◽  
T.H. Moss ◽  
R.H. Holm ◽  
...  
Keyword(s):  
Structural Variation ◽  
Resonance Raman ◽  
Spectroscopic Evidence ◽  
Raman Spectroscopic ◽  
Bacterial Ferredoxin

An X-ray investigation of the structure of a bacterial ferredoxin

1965 ◽  
Vol 20 (1) ◽  
pp. 33-35 ◽  
Author(s):  
L.C. Sieker ◽  
L.H. Jensen
Keyword(s):  
X Ray ◽  
Bacterial Ferredoxin

INVESTIGATION OF BACTERIAL FERREDOXIN BY MÖSSBAUER SPECTROSCOPY

1974 ◽  
Vol 35 (C6) ◽  
pp. C6-367-C6-370
Author(s):  
H. EICHER ◽  
F. PARAK ◽  
L. BOGNER ◽  
D. BADE ◽  
G. M. KALVIUS ◽  
...  
Keyword(s):  
Mössbauer Spectroscopy ◽  
Mossbauer Spectroscopy ◽  
Mößbauer Spectroscopy ◽  
Bacterial Ferredoxin

A new catalytic mechanism of bacterial ferredoxin‐NADP + reductases due to a particular NADP + binding mode

2021 ◽  
Author(s):  
Paula Monchietti ◽  
Arleth S. López Rivero ◽  
Eduardo A. Ceccarelli ◽  
Daniela L. Catalano‐Dupuy
Keyword(s):  
Catalytic Mechanism ◽  
Binding Mode ◽  
Bacterial Ferredoxin

scholarly journals The Structure of a Bacterial Ferredoxin

1973 ◽  
Vol 248 (11) ◽  
pp. 3987-3996 ◽  
Author(s):  
Elinor T. Adman ◽  
Larry C. Sieker ◽  
Lyle H. Jensen
Keyword(s):  
Bacterial Ferredoxin

Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases

2004 ◽  
Vol 1698 (2) ◽  
pp. 155-165 ◽  
Author(s):  
Eduardo A. Ceccarelli ◽  
Adrián K. Arakaki ◽  
Néstor Cortez ◽  
Néstor Carrillo
Keyword(s):  
Catalytic Efficiency ◽  
Functional Plasticity ◽  
Bacterial Ferredoxin

Arabidopsis FNRL protein is an NADPH‐dependent chloroplast oxidoreductase resembling bacterial ferredoxin‐NADP + reductases

2017 ◽  
Vol 162 (2) ◽  
pp. 177-190 ◽  
Author(s):  
Minna M. Koskela ◽  
Käthe M. Dahlström ◽  
Guillermina Goñi ◽  
Nina Lehtimäki ◽  
Markus Nurmi ◽  
...  
Keyword(s):  
Bacterial Ferredoxin
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