Search

Your search keyword '"Rasmussen, Tim"' showing total 8 results
Start Over Author "Rasmussen, Tim" Journal biochemistry
8 results on '"Rasmussen, Tim"'

1. Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I)

Author

Rasmussen, Tim, Scheide, Dierk, Brors, Benedikt, Kintscher, Lars, Weiss, Hanns, and Friedrich, Thorsten

Subjects
Enzymes -- Structure-activity relationship, Oxidation-reduction reaction -- Physiological aspects, Neurospora -- Research, Binding sites (Biochemistry) -- Analysis, Bioenergetics -- Research, Biological sciences, Chemistry
Abstract

Research demonstrates a second novel redox group in complex I of Neurospora crassa and Escherichia coli in addition to the one previously reported. The redox group is composed of two tetranuclear FeS clusters, exhibits a pH-independent midpoint potential of -270 mV, and is capable of transferring two electrons.

Published
2001

2. The role of tryptophan residues in the function and stability of the mechanosensitive channel MscS from Escherichia coli

Author

Rasmussen, Akiko, Rasmussen, Tim, Edwards, Michelle D., Schauer, Daniela, Schumann, Ulrike, Miller, Samantha, and Booth, Ian R.

Subjects
Escherichia coli -- Genetic aspects, Mutagenesis -- Usage, Biological sciences, Chemistry
Abstract

Site-directed mutagenesis was used for examining the role of tryptophan (Trp) residues in MscS function. Results suggest that Trp residue W16 plays a significant role in the gating of MscS, whereas Trp residue W240 plays an essential role in MscS oligomer stability.

Published
2007

3. Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificans Kef Potassium Efflux System

Author

Pliotas, Christos, primary, Grayer, Samuel C., additional, Ekkerman, Silvia, additional, Chan, Anthony K. N., additional, Healy, Jess, additional, Marius, Phedra, additional, Bartlett, Wendy, additional, Khan, Amjad, additional, Cortopassi, Wilian A., additional, Chandler, Shane A., additional, Rasmussen, Tim, additional, Benesch, Justin L. P., additional, Paton, Robert S., additional, Claridge, Timothy D. W., additional, Miller, Samantha, additional, Booth, Ian R., additional, Naismith, James H., additional, and Conway, Stuart J., additional

Published
2017
Full Text
View/download PDF

6. Adenosine Monophosphate Binding Stabilizes the KTN Domain of the Shewanella denitrificansKef Potassium Efflux System

Author

Pliotas, Christos, Grayer, Samuel C., Ekkerman, Silvia, Chan, Anthony K. N., Healy, Jess, Marius, Phedra, Bartlett, Wendy, Khan, Amjad, Cortopassi, Wilian A., Chandler, Shane A., Rasmussen, Tim, Benesch, Justin L. P., Paton, Robert S., Claridge, Timothy D. W., Miller, Samantha, Booth, Ian R., Naismith, James H., and Conway, Stuart J.

Abstract

Ligand binding is one of the most fundamental properties of proteins. Ligand functions fall into three basic types: substrates, regulatory molecules, and cofactors essential to protein stability, reactivity, or enzyme–substrate complex formation. The regulation of potassium ion movement in bacteria is predominantly under the control of regulatory ligands that gate the relevant channels and transporters, which possess subunits or domains that contain Rossmann folds (RFs). Here we demonstrate that adenosine monophosphate (AMP) is bound to both RFs of the dimeric bacterial Kef potassium efflux system (Kef), where it plays a structural role. We conclude that AMP binds with high affinity, ensuring that the site is fully occupied at all times in the cell. Loss of the ability to bind AMP, we demonstrate, causes protein, and likely dimer, instability and consequent loss of function. Kef system function is regulated via the reversible binding of comparatively low-affinity glutathione-based ligands at the interface between the dimer subunits. We propose this interfacial binding site is itself stabilized, at least in part, by AMP binding.

Published
2017
Full Text
View/download PDF

8. The Catalytic Center in Nitrous Oxide Reductase, Cu[sub z], Is a Copper--Sulfide Cluster.

Author

Rasmussen, Tim and Berks, Ben C.

Subjects
*ENZYMES, *LIGANDS (Biochemistry), *RAMAN spectroscopy
Abstract

Identifies Cu[sub z], the catalytic center in nitrous oxide reductase as a copper--sulfide cluster. Application of Raman spectroscopy in the study; Isolation of the reductase from the bacteria Paracoccus pantotrophus and Pseudomonas stutzeri; Existence of an acid-labile sulfur ligand in the catalytic center.

Published
2000
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results