Ann Magnuson

[FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy

Németh, Brigitta; Senger, Moritz; Redman, Holly J.; Ceccaldi, Pierre et al.

Ingår i Journal of Biological Inorganic Chemistry, s. 777-788, 2020

• DOI för [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy
• Ladda ner fulltext (pdf) av [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy

The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions

Németh, Brigitta; Land, Henrik; Magnuson, Ann; Hofer, Anders et al.

Ingår i Journal of Biological Chemistry, s. 11891-11901, 2020

• DOI för The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
• Ladda ner fulltext (pdf) av The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions

Heterocyst Thylakoid Bioenergetics

Magnuson, Ann

Ingår i Life, 2019

• DOI för Heterocyst Thylakoid Bioenergetics
• Ladda ner fulltext (pdf) av Heterocyst Thylakoid Bioenergetics

Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading

Rozman Grinberg, Inna; Berglund, Sigrid; Hasan, Mahmudul; Lundin, Daniel et al.

Ingår i Journal of Biological Inorganic Chemistry, s. 863-877, 2019

• DOI för Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading
• Ladda ner fulltext (pdf) av Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading

Thylakoid membrane function in heterocysts

Magnuson, Ann; Cardona, Tanai

Ingår i Biochimica et Biophysica Acta - Bioenergetics, s. 309-319, 2016

• DOI för Thylakoid membrane function in heterocysts

Turning around the electron flow in an uptake hydrogenase. EPR spectroscopy and in vivo activity of a designed mutant in HupSL from Nostoc punctiforme

Raleiras, Patrícia; Khanna, Namita; Miranda, Helder; Meszaros, Livia S. et al.

Ingår i Energy & Environmental Science, s. 581-594, 2016

• DOI för Turning around the electron flow in an uptake hydrogenase. EPR spectroscopy and in vivo activity of a designed mutant in HupSL from Nostoc punctiforme

Isolation and Characterization of the Small Subunit of the Uptake Hydrogenase from the Cyanobacterium Nostoc punctiforme.

Raleiras, Patricia; Kellers, Petra; Lindblad, Peter; Styring, Stenbjörn et al.

Ingår i Journal of Biological Chemistry, s. 18345-18352, 2013

• DOI för Isolation and Characterization of the Small Subunit of the Uptake Hydrogenase from the Cyanobacterium Nostoc punctiforme.

Artificial Photosynthesis for Solar Fuels – an Evolving Research Field within AMPEA, a Joint Programme of the European Energy Research Alliance

Thapper, Anders; Styring, Stenbjörn; Saracco, Guido; Rutherford, A. William et al.

Ingår i Green, s. 43-57, 2013

• DOI för Artificial Photosynthesis for Solar Fuels – an Evolving Research Field within AMPEA, a Joint Programme of the European Energy Research Alliance

Modeling Photosystem I with the alternative reaction center protein PsaB2 in the nitrogen fixing cyanobacterium Nostoc punctiforme

Magnuson, Ann; Krassen, Henning; Stensjö, Karin; Ho, Felix M. et al.

Ingår i Biochimica et Biophysica Acta - Bioenergetics, s. 1152-1161, 2011

• DOI för Modeling Photosystem I with the alternative reaction center protein PsaB2 in the nitrogen fixing cyanobacterium Nostoc punctiforme

Hydrogen production by a fully de novo enzyme

Berglund, Sigrid; Bassy, Clara; Kaya, Ibrahim; Andrén, Per E. et al.

Ingår i Dalton Transactions, s. 12905-12916, 2024

• DOI för Hydrogen production by a fully de novo enzyme
• Ladda ner fulltext (pdf) av Hydrogen production by a fully de novo enzyme

[FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy

Németh, Brigitta; Senger, Moritz; Redman, Holly J.; Ceccaldi, Pierre et al.

Ingår i Journal of Biological Inorganic Chemistry, s. 777-788, 2020

• DOI för [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy
• Ladda ner fulltext (pdf) av [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy

The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions

Németh, Brigitta; Land, Henrik; Magnuson, Ann; Hofer, Anders et al.

Ingår i Journal of Biological Chemistry, s. 11891-11901, 2020

• DOI för The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
• Ladda ner fulltext (pdf) av The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions

Heterocyst Thylakoid Bioenergetics

Magnuson, Ann

Ingår i Life, 2019

• DOI för Heterocyst Thylakoid Bioenergetics
• Ladda ner fulltext (pdf) av Heterocyst Thylakoid Bioenergetics

Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading

Rozman Grinberg, Inna; Berglund, Sigrid; Hasan, Mahmudul; Lundin, Daniel et al.

Ingår i Journal of Biological Inorganic Chemistry, s. 863-877, 2019

• DOI för Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading
• Ladda ner fulltext (pdf) av Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading

Hydrogen production by a fully de novo enzyme

Berglund, Sigrid; Bassy, Clara; Kaya, Ibrahim; Andrén, Per E. et al.

Ingår i Dalton Transactions, s. 12905-12916, 2024

• DOI för Hydrogen production by a fully de novo enzyme
• Ladda ner fulltext (pdf) av Hydrogen production by a fully de novo enzyme

[FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy

Németh, Brigitta; Senger, Moritz; Redman, Holly J.; Ceccaldi, Pierre et al.

Ingår i Journal of Biological Inorganic Chemistry, s. 777-788, 2020

• DOI för [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy
• Ladda ner fulltext (pdf) av [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy

The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions

Németh, Brigitta; Land, Henrik; Magnuson, Ann; Hofer, Anders et al.

Ingår i Journal of Biological Chemistry, s. 11891-11901, 2020

• DOI för The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
• Ladda ner fulltext (pdf) av The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions

Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading

Rozman Grinberg, Inna; Berglund, Sigrid; Hasan, Mahmudul; Lundin, Daniel et al.

Ingår i Journal of Biological Inorganic Chemistry, s. 863-877, 2019

• DOI för Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading
• Ladda ner fulltext (pdf) av Class Id ribonucleotide reductase utilizes a Mn₂(IV,III) cofactor and undergoes large conformational changes on metal loading

Turning around the electron flow in an uptake hydrogenase. EPR spectroscopy and in vivo activity of a designed mutant in HupSL from Nostoc punctiforme

Raleiras, Patrícia; Khanna, Namita; Miranda, Helder; Meszaros, Livia S. et al.

Ingår i Energy & Environmental Science, s. 581-594, 2016

• DOI för Turning around the electron flow in an uptake hydrogenase. EPR spectroscopy and in vivo activity of a designed mutant in HupSL from Nostoc punctiforme

Isolation and Characterization of the Small Subunit of the Uptake Hydrogenase from the Cyanobacterium Nostoc punctiforme.

Raleiras, Patricia; Kellers, Petra; Lindblad, Peter; Styring, Stenbjörn et al.

Ingår i Journal of Biological Chemistry, s. 18345-18352, 2013

• DOI för Isolation and Characterization of the Small Subunit of the Uptake Hydrogenase from the Cyanobacterium Nostoc punctiforme.

Artificial Photosynthesis for Solar Fuels – an Evolving Research Field within AMPEA, a Joint Programme of the European Energy Research Alliance

Thapper, Anders; Styring, Stenbjörn; Saracco, Guido; Rutherford, A. William et al.

Ingår i Green, s. 43-57, 2013

• DOI för Artificial Photosynthesis for Solar Fuels – an Evolving Research Field within AMPEA, a Joint Programme of the European Energy Research Alliance

Modeling Photosystem I with the alternative reaction center protein PsaB2 in the nitrogen fixing cyanobacterium Nostoc punctiforme

Magnuson, Ann; Krassen, Henning; Stensjö, Karin; Ho, Felix M. et al.

Ingår i Biochimica et Biophysica Acta - Bioenergetics, s. 1152-1161, 2011

• DOI för Modeling Photosystem I with the alternative reaction center protein PsaB2 in the nitrogen fixing cyanobacterium Nostoc punctiforme

Heterocyst Thylakoid Bioenergetics

Magnuson, Ann

Ingår i Life, 2019

• DOI för Heterocyst Thylakoid Bioenergetics
• Ladda ner fulltext (pdf) av Heterocyst Thylakoid Bioenergetics

Thylakoid membrane function in heterocysts

Magnuson, Ann; Cardona, Tanai

Ingår i Biochimica et Biophysica Acta - Bioenergetics, s. 309-319, 2016

• DOI för Thylakoid membrane function in heterocysts

Probing substrate water access through the O1 channel of Photosystem II by single site mutations and membrane inlet mass spectrometry

Aydin, Abuzer Orkun; de Lichtenberg, Casper; Liang, Feiyan; Forsman, Jack et al.