H. Ooka

Thermodynamics Underpinning the Microbial Community-Level Nitrogen Networks

This study identifies energetically superior nitrogen reactions in microbial communities by analyzing 988 potential redox reactions and showing their alignment with observed microbial nitrogen networks.

Diverse Phosphoserine Phosphatases Exhibit Maximum Activity at an Intermediate Binding Affinity in Accord with the Sabatier Principle of Catalysis

This paper shows that phosphoserine phosphatases exhibit maximum activity at an intermediate binding affinity, supporting the Sabatier principle of catalysis when considering both Km and the product release rate constant.

Universal Design Principle to Enhance Enzymatic Activity using the Substrate Affinity

The paper demonstrates that setting the Michaelis-Menten constant (Km) equal to substrate concentration (S) maximizes enzymatic activity, providing a quantitative guideline for enzyme optimization.