Page last updated: 2024-08-23

protochlorophyllide and lysine

protochlorophyllide has been researched along with lysine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Karginova, O; Lebedev, N; McIvor, W; Timko, MP	1
Bröcker, MJ; Ganskow, S; Heathcote, P; Heinz, DW; Jahn, D; Moser, J; Schubert, WD; Virus, S	1

Other Studies

2 other study(ies) available for protochlorophyllide and lysine

Article	Year
Tyr275 and Lys279 stabilize NADPH within the catalytic site of NADPH:protochlorophyllide oxidoreductase and are involved in the formation of the enzyme photoactive state. Biochemistry, 2001, Oct-23, Volume: 40, Issue:42 Topics: Amino Acid Substitution; Binding Sites; Catalytic Domain; Enzyme Activation; Enzyme Stability; Freezing; Kinetics; Lysine; Mutagenesis, Site-Directed; NADP; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Photochemistry; Pisum sativum; Protein Denaturation; Protochlorophyllide; Rhodobacter capsulatus; Spectrometry, Fluorescence; Substrate Specificity; Temperature; Tyrosine	2001
ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis. The Journal of biological chemistry, 2008, Apr-18, Volume: 283, Issue:16 Topics: Adenosine Triphosphate; Catalysis; Chlorobium; Cysteine; Dithionite; Electrons; Escherichia coli; Heme; Kinetics; Leucine; Light; Lysine; Nitrogenase; Oxidoreductases; Protochlorophyllide	2008

Article

Year

Tyr275 and Lys279 stabilize NADPH within the catalytic site of NADPH:protochlorophyllide oxidoreductase and are involved in the formation of the enzyme photoactive state.

Biochemistry, 2001, Oct-23, Volume: 40, Issue:42

Topics: Amino Acid Substitution; Binding Sites; Catalytic Domain; Enzyme Activation; Enzyme Stability; Freezing; Kinetics; Lysine; Mutagenesis, Site-Directed; NADP; Oxidoreductases; Oxidoreductases Acting on CH-CH Group Donors; Photochemistry; Pisum sativum; Protein Denaturation; Protochlorophyllide; Rhodobacter capsulatus; Spectrometry, Fluorescence; Substrate Specificity; Temperature; Tyrosine

2001

ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis.

The Journal of biological chemistry, 2008, Apr-18, Volume: 283, Issue:16

Topics: Adenosine Triphosphate; Catalysis; Chlorobium; Cysteine; Dithionite; Electrons; Escherichia coli; Heme; Kinetics; Leucine; Light; Lysine; Nitrogenase; Oxidoreductases; Protochlorophyllide

2008